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Metabolites  2014 

Regulation Systems of Bacteria such as Escherichia coli in Response to Nutrient Limitation and Environmental Stresses

DOI: 10.3390/metabo4010001

Keywords: metabolic regulation, nutrient limitation, environmental stress, intracellular metabolite, global regulators, enzyme level regulation, transcriptional regulation

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Abstract:

An overview was made to understand the regulation system of a bacterial cell such as Escherichia coli in response to nutrient limitation such as carbon, nitrogen, phosphate, sulfur, ion sources, and environmental stresses such as oxidative stress, acid shock, heat shock, and solvent stresses. It is quite important to understand how the cell detects environmental signals, integrate such information, and how the cell system is regulated. As for catabolite regulation, F1,6B P (FDP), PEP, and PYR play important roles in enzyme level regulation together with transcriptional regulation by such transcription factors as Cra, Fis, CsrA, and cAMP-Crp. αKG plays an important role in the coordinated control between carbon (C)- and nitrogen (N)-limitations, where αKG inhibits enzyme I (EI) of phosphotransferase system (PTS), thus regulating the glucose uptake rate in accordance with N level. As such, multiple regulation systems are co-ordinated for the cell synthesis and energy generation against nutrient limitations and environmental stresses. As for oxidative stress, the TCA cycle both generates and scavenges the reactive oxygen species (ROSs), where NADPH produced at ICDH and the oxidative pentose phosphate pathways play an important role in coping with oxidative stress. Solvent resistant mechanism was also considered for the stresses caused by biofuels and biochemicals production in the cell.

References

[1]  Seshasayee, A.S.; Bertone, P.; Fraser, G.M.; Luscombe, N.M. Transcriptional regulatory networks in bacteria: From input signals to output responses. Curr. Opin. Microbiol. 2006, 9, 511–519, doi:10.1016/j.mib.2006.08.007.
[2]  Kitano, H. Systems biology: A brief overview. Science 2002, 295, 1662–1664, doi:10.1126/science.1069492.
[3]  Kitano, H. Computational systems biology. Nature 2002, 420, 206–210, doi:10.1038/nature01254.
[4]  Kotte, O.; Zaugg, J.B.; Heinemann, M. Bacterial adaptation through distributed sensing of metabolic fluxes. Mol. Syst. Biol. 2010, 6, 355.
[5]  Kanehisa, M.; Goto, S.; Hattori, M.; Aoki-Kinoshita, K.F.; Itoh, M.; Kawashima, S.; Katayama, T.; Araki, M.; Hirakawa, M. From genomics to chemical genomics: New developments in KEGG. Nucleic Acids Res. 2006, 34, D354–D357, doi:10.1093/nar/gkj102.
[6]  Yamamoto, K.; Hirao, K.; Oshima, T.; Aiba, H.; Utsumi, R.; Ishihama, A. Functional characterization in vitro of all two component signal transduction systems from Escherichia coli. J. Biol. Chem. 2005, 280, 1448–1456.
[7]  Maeda, H.; Fujita, N.; Ishihama, A. Competition among seven Escherichia coli sigma subunits: Relative binding affi nities to the core RNA polymerase. Nucleic Acids Res. 2000, 28, 3497–3503, doi:10.1093/nar/28.18.3497.
[8]  Timmermans, J.; van Melderen, L. Post-transcriptional global regulation by CsrA in bacteria. Cell. Mol. Life Sci. 2010, 67, 2897–2908, doi:10.1007/s00018-010-0381-z.
[9]  Bruckner, R.; Titgemeyer, F. Carbon catabolite repression in bacteria: Choice of the carbon source and autoregulatory limitation of sugar utilization. FEMS Microbiol. Lett. 2002, 209, 141–148, doi:10.1016/S0378-1097(02)00559-1.
[10]  Gutierrez-RiosR, M.; Freyre-Gonzalez, J.A.; Resendis, O.; Collado-Vides, J.; Saier, M.; Gosset, G. Identification of regulatory network topological units coordinating the genome-wide transcriptional response to glucose in Escherichia coli. BMC Microbiol. 2007, 7, 53, doi:10.1186/1471-2180-7-53.
[11]  De Lay, N.; Gottesman, S. The crp-activated small noncoding regulatory RNA CyaR (RyeE) links nutritional status to group behavior. J. Bacteriol. 2009, 191, 461–476, doi:10.1128/JB.01157-08.
[12]  Muller, C.M.; Aberg, A.; Straseviciene, J.; Emody, L.; Uhlin, B.E.; Balsalobre, C. Type 1 fimbriae, a colonization factor of uropathogenic Escherichia coli, are controlled by the metabolic sensor CRP-cAMP. PLoS Pathog. 2009, 5, e1000303, doi:10.1371/journal.ppat.1000303.
[13]  Zheng, D.; Constantinidou, C.; Hobman, J.L.; Minchin, S.D. Identification of the CRP regulon using in vitro and in vivo transcriptional profiling. Nucleic Acids Res. 2004, 32, 5874–5893, doi:10.1093/nar/gkh908.
[14]  Gottesman, S. Micros for microbes: Non-coding regulatory RNAs in bacteria. Trends Genet. 2005, 21, 399–404, doi:10.1016/j.tig.2005.05.008.
[15]  Vanderpool, C.K.; Gottesman, S. Involvement of a novel transcriptional activator and smallRNA in post-transcriptional regulation of the glucose phosphoenolpyruvate phosphotransferase system. Mol. Microbiol. 2004, 54, 1076–1089, doi:10.1111/j.1365-2958.2004.04348.x.
[16]  Babitzke, P.; Romeo, T. CsrB sRNA family: Sequestration of RNA-binding regulatory proteins. Curr. Opin. Microbiol. 2007, 10, 156–163, doi:10.1016/j.mib.2007.03.007.
[17]  Sauer, E.; Weichenrieder, O. Structural basis for RNA 3'-end recognition by Hfq. Proc. Natl. Acad. Sci. USA 2011, 108, 13065–13070, doi:10.1073/pnas.1103420108.
[18]  Sauer, E.; Schmidt, S.; Weichenrieder, O. Small RNA binding to the lateral surface of Hfq hexamers and structural rearrangements upon mRNA target recognition. Proc. Natl. Acad. Sci. USA 2012, 109, 9396–9401, doi:10.1073/pnas.1202521109.
[19]  Voge, J.; Luis, B.F. Hfq and its constellation of RNA. Nat. Rev. Microbiol. 2011, 9, 578–589, doi:10.1038/nrmicro2615.
[20]  Shimizu, K. Bacterial Cellular Metabolic Systems; Woodhead Publ. Co.: Oxford, UK, 2013.
[21]  Shimizu, K. Metabolic regulation of a bacterial cell system with emphasis on Escherichia coli metabolism. ISRN Biochem. 2013, 645983:1–645983:47.
[22]  Simon, S.A.; Gutknecht, J. Solubility of carbon dioxide in lipid bilayer membranes and organic solvents. Biochim. Biophys. Acta 1980, 596, 352–358, doi:10.1016/0005-2736(80)90122-4.
[23]  Walter, A.; Gutknecht, J. Permeability of small nonelectrolytes through lipid bilayer membranes. J. Membr. Biol. 1986, 90, 207–217, doi:10.1007/BF01870127.
[24]  Nikaido, H.; Nakae, T. The outer membrane of gram-negative bacteria. Adv. Microb. Physiol. 1980, 20, 163–250, doi:10.1016/S0065-2911(08)60208-8.
[25]  De la Cruz, M.A.; Fernandez-Mora, M.; Guadarrama, C.; Flores-Valdez, M.A.; Bustamante, V.H.; Vázquez, A.; Calva, E. LeuO antagonizes H-NS and StpA-dependent repression in Salmonella entericaompS1. Mol. Microbiol. 2007, 66, 727–743, doi:10.1111/j.1365-2958.2007.05958.x.
[26]  Nikaido, H. Molecular basis of bacterial outer membrane permeability revisited. Microbiol. Mol. Biol. Rev. 2003, 67, 593–656, doi:10.1128/MMBR.67.4.593-656.2003.
[27]  Nikaido, H. Outer Membrane; Neidhardt, F.C., Ed.; ASM Press: Washington, DC, USA, 1996.
[28]  Death, A.; Ferenci, T. Between feast and famine: Endogenous inducer synthesis in the adaptation of Escherichia coli to growth with limiting carbohydrates. J. Bacteriol. 1994, 176, 5101–5107.
[29]  Von Meyenburg, K.; Nikaido, H. Outer membrane of gramnegative bacteria. XVII. Specificity of transport process catalyzed by the λ-receptor protein in Escherichia coli. Biochem. Biophys. Res. Commun. 1977, 78, 1100–1107, doi:10.1016/0006-291X(77)90534-4.
[30]  Brzostek, K.; Brzostkowska, M.; Bukowska, I.; Karwicka, E.; Raczkowska, A. OmpR negatively regulates expression of invasion in Yersinia enterocolitica. Microbiology 2007, 153, 2416–2425, doi:10.1099/mic.0.2006/003202-0.
[31]  Gunnewijk, M.G.W.; van den Bogaard, P.T.C.; Veenhoff, L.M.; Heuberger, E.H.; de Vos, W.M.; Kleerebezem, M.; Kuipers, O.P.; Poolman, B. Hierarchical control versus autoregulation of carbohydrate utilization in bacteria. J. Mol. Microbiol. Biotechnol. 2001, 3, 401–413.
[32]  Postma, P.W.; Lengeler, J.W.; Jacobson, G.R. Phosphoenolpyruvate: Carbohydrate Phosphotransferase Systems. In Escherichia coli and Salmonella: Cellular and Molecular Biology; Neidhardt, F.C., Ed.; ASM Press: Washington, DC, USA, 1996; pp. 1149–1174.
[33]  Tchieu, J.H.; Norris, V.; Edwards, J.S.; Saier, M.H., Jr. The complete phosphotransferase system in Escherichia coli. J. Mol. Microbiol. Biotechnol. 2001, 3, 329–346.
[34]  Chou, C.H.; Bennett, G.N.; San, K.Y. Effect ofmodulated glucose uptake on high-level recombinant protein production in a dense Escherichia coli culture. Biotechnol. Prog. 1994, 10, 644–647, doi:10.1021/bp00030a009.
[35]  Gosset, G. Improvement of Escherichia coli production strains by modification of the phosphoenolpyruvate: Sugar phosphotransferase system. Microb. Cell Fact. 2005, 4, 14, doi:10.1186/1475-2859-4-14.
[36]  Lunin, V.V.; Li, Y.; Schrag, J.D.; Iannuzzi, P.; Cygler, M.; Matte, A. Crystal structures of Escherichia coli ATP-dependent glucokinase and its complex with glucose. J. Bacteriol. 2004, 186, 6915–6927, doi:10.1128/JB.186.20.6915-6927.2004.
[37]  Huberts, D.H.; Niebel, B.; Heinemann, M. A flux-sensing mechanism could regulate the switch between respiration and fermentation. FEMS Yeast Res. 2012, 12, 118–128, doi:10.1111/j.1567-1364.2011.00767.x.
[38]  Kochanowski, K.; Volkmer, B.; Gerosa, L.; van Rijsewijk, H.B.R.; Schmidt, A.; Heinemann, M. Functioning of a metabolic flux sensor in Escherichia coli. Proc. Natl. Acad. Sci. USA 2013, 110, 1130–1135, doi:10.1073/pnas.1202582110.
[39]  Valgepea, K.; Adamberg, K.; Nahku, R.; Lahtvee, P.J.; Arike, L.; Vilu, R. Systems biology approach reveals that overflow metabolism of acetate in Escherichia coli is triggered by carbon catabolite repression of acetyl-CoA synthetase. BMC Syst. Biol. 2010, 4, 166, doi:10.1186/1752-0509-4-166.
[40]  Valgepea, K.; Adamberg, K.; Vilu, R. Decrease of energy spilling in Escherichia coli continuous cultures with rising specific growth rate and carbon wasting. BMC Syst. Biol. 2011, 5, 106, doi:10.1186/1752-0509-5-106.
[41]  Kayser, A.; Weber, J.; Hecht, V.; Rinas, U. Metabolic flux analysis of Escherichia coli in glucose-limited continuous culture. I. Growth-rate dependent metabolic efficiency at steady state. Microbiology 2005, 151, 693–706.
[42]  Nachen, A.; Schicker, A.; Revelles, O.; Sauer, U. Cyclic AMP-dependent catabolite repression is the dominant control mechanism of metabolic fluxes under glucose limitation in Escherichia coli. J. Biotechnol. 2008, 190, 2323–2330.
[43]  Hua, Q.; Yang, C.; Baba, T.; Mori, H.; Shimizu, K. Responses of the central carbon metabolism in Escherichia coli to phosphoglucose isomerase and glucose-6-phosphate dehydrogenase knockouts. J. Bacteriol. 2003, 185, 7053–7067, doi:10.1128/JB.185.24.7053-7067.2003.
[44]  Bettenbrock, K.; Sauter, T.; Jahreis, K.; Klemling, A.; Lengeler, J.W.; Gilles, E.D. Correlation be-tween growth rates, EIIACrr phosphorylation, and intra-cellular cyclic AMP levels in Escherichia coli K-12. J. Bacteriol. 2007, 189, 6891–6900, doi:10.1128/JB.00819-07.
[45]  Hogema, B.M.; Arents, J.C.; Bader, R.; Eijkemans, K.; Yoshida, H.; Takahashi, H.; Aiba, H.; Postma, P.W. Inducer exclusion in Escherichia coli by non-PTS substrates: The role of the PEP to pyruvate ratio in deter-mining the phosphorylation state of enzyme IIAGlc. Mol. Microbiol. 1998, 30, 487–498, doi:10.1046/j.1365-2958.1998.01053.x.
[46]  Matsuoka, Y.; Shimizu, K. Catabolite regulation analysis of Escherichia coli for acetate overflow mechanism and co-consumption of multiple sugars based on systems biology approach using computer simulation. J. Biotechnol. 2013, 168, 155–173, doi:10.1016/j.jbiotec.2013.06.023.
[47]  Yao, R.; Hirose, Y.; Sarkar, D.; Nakahigashi, K.; Ye, Q.; Shimizu, K. Catabolic regulation analysis of Escherichia coli and its crp, mlc, mgsA, pgi and ptsG mutants. Microb. Cell Fact. 2011, 10, 67, doi:10.1186/1475-2859-10-67.
[48]  Ishii, N.; Nakahigashi, K.; Baba, T.; Robert, M.; Soga, T.; Kanai, A.; Hirasawa, T.; Naba, M.; Hirai, K.; Hoque, A.; et al. Multiple high-throughput analyses monitor the response of E. coli to perturbations. Science 2007, 316, 593–597, doi:10.1126/science.1132067.
[49]  Brauer, M.J.; Yuan, J.; Bennett, B.D.; Lu, W.; Kimball, E.; Botstein, D.; Rabinowitz, J.D. Conservation of the metabolomic response to starvation across two divergent microbes. Proc. Natl. Acad. Sci. USA 2006, 103, 19302–19307, doi:10.1073/pnas.0609508103.
[50]  Zampar, G.G.; Kümmel, A.; Ewald, J.; Jol, S.; Niebel, B.; Picotti, P.; Aebersold, R.; Sauer, U.; Zamboni, N.; Heinemann, M. Temporal system-level organization of the switch from glycolytic to gluconeogenic operation in yeast. Mol. Syst.Biol. 2013, 9, 651.
[51]  Romeo, T. Global regulation by the small RNA-binding protein CsrA and the non- coding RNA molecule CsrB. Mol. Microbiol. 1998, 29, 1321–1330, doi:10.1046/j.1365-2958.1998.01021.x.
[52]  Jonas, K.; Edwards, A.N.; Ahmad, I.; Romeo, T.; Romling, U.; Melefors, O. Complex regulatory network encompassing the Csr, c-di-GMP and motility systems of Salmonella typhimurium. Environ. Microbiol. 2010, 12, 524–540, doi:10.1111/j.1462-2920.2009.02097.x.
[53]  Yakhnin, H.; Pandit, P.; Petty, T.J.; Baker, C.S.; Romeo, T.; Babitzke, P. CsrA of Bacillus subtilis regulates translation initiation of the gene encoding the flagellin protein (hag) by blocking ribosome binding. Mol. Microbiol. 2007, 64, 1605–1620, doi:10.1111/j.1365-2958.2007.05765.x.
[54]  Romeo, T.; Gong, M. Genetic and physical mapping of the regulatory gene csrA on the Escherichia coli K-12 chromosome. J. Bacteriol. 1993, 175, 5740–5741.
[55]  Romeo, T.; Gong, M.; Liu, M.Y.; Brun-Zinkernagel, A.M. Identification and molecular characterization of csrA, a pleiotropic gene from Escherichia coli that affects glycogen biosynthesis, gluconeogenesis, cell size, and surface properties. J. Bacteriol. 1993, 175, 4744–4755.
[56]  Romeo, T. Post-transcriptional regulation of bacterial carbohydratemetabolism: Evidence that the gene productCsrA is global mRNA decay factor. Res. Microbiol. 1996, 147, 505–512, doi:10.1016/0923-2508(96)84004-6.
[57]  Dubey, A.K.; Baker, C.S.; Romeo, T.; Babitzke, P. RNA sequence and secondary structure participate in high-affinity CsrA-RNA interaction. RNA 2005, 11, 1579–1587, doi:10.1261/rna.2990205.
[58]  Suzuki, K.; Wang, X.; Weilbacher, T.; Pernestig, A.K.; Melefors, O.; Georgellis, D.; Babitzke, P.; Romeo, T. Regulatory circuitry of the CsrA/CsrB and BarA/UvrY systems of Escherichia coli. J. Bacteriol. 2002, 184, 5130–5140, doi:10.1128/JB.184.18.5130-5140.2002.
[59]  Weilbacher, T.; Suzuki, K.; Dubey, A.K.; Wang, X.; Gudapaty, S.; Morozov, I.; Baker, C.S.; Georgellis, D.; Babitzke, P.; Romeo, T. A novel sRNA component of the carbon storage regulatory system of Escherichia coli. Mol. Microbiol. 2003, 48, 657–670, doi:10.1046/j.1365-2958.2003.03459.x.
[60]  Baker, C.S.; Morozov, I.; Suzuki, K.; Romeo, T.; Babitzke, P. CsrA regulates glycogen biosynthesis by preventing translation of glgC in Escherichia coli. Mol. Microbiol. 2002, 44, 1599–1610, doi:10.1046/j.1365-2958.2002.02982.x.
[61]  McKee, A.E.; Rutherford, B.J.; Chivian, D.C.; Baidoo, E.K.; Juminaga, D.; Kuo, D.; Benke, P.I.; Dietrich, J.A.; Ma, S.M.; Arkin, A.P.; et al. Manipulation of the carbon storage regulator system for metabolite remodeling and biofuel production in Escherichia coli. Microb. Cell Fact. 2012, 11, 79, doi:10.1186/1475-2859-11-79.
[62]  Tatarko, M.; Romeo, T. Disruption of a global regulatory gene to enhance CEntral carbon flux into Phenylalanine biosynthesis in Escherichia coli. Curr. Microbiol. 2001, 43, 26–32, doi:10.1007/s002840010255.
[63]  Edwards, A.N.; Patterson-Fortin, L.M.; Vakulskas, C.A.; Mercante, J.W.; Potrykus, K.; Vinella, D.; Camacho, M.I.; Fields, J.A.; Thompson, S.A.; Georgellis, D.; et al. Circuitry linking the Csr and stringent response global regulatory systems. Mol. Microbiol. 2011, 80, 1561–1580, doi:10.1111/j.1365-2958.2011.07663.x.
[64]  Yan, D. Protection of the glutamate pool concentration in enteric bacteria. Proc. Natl. Acad. Sci. USA 2007, 104, 9475–9480, doi:10.1073/pnas.0703360104.
[65]  Ninfa, A.J.; Jiang, P.; Atkinson, M.R.; Peliska, J.A. Integration of antagonistic signals in the regulation of nitrogen assimilation in Escherichia coli. Curr. Topics Cell. Regul. 2000, 36, 31–75.
[66]  Gruswitz, F.; O’Connell, J.; Stroud, R.M. Inhibitory complex of the transmembrane ammonia channel, AmtB, and the cytosolic regulatory protein, GlnK, at 1.96 A. Proc. Natl. Acad. Sci. USA 2007, 104, 42–47, doi:10.1073/pnas.0609796104.
[67]  Radchenko, M.V.; Thornton, J.; Merrick, M. Control of AmtB-GlnK complex formation by intracellular levels of ATP, ADP, and 2-oxoglutarate. J. Biol. Chem. 2010, 285, 31037–31045, doi:10.1074/jbc.M110.153908.
[68]  Truan, D.; Huergo, L.F.; Chubatsu, L.S.; Merrick, M.; Li, X.D.; Winkler, F.K. A new P(II) protein structure identifies the 2-oxoglutarate binding site. J. Mol. Biol. 2010, 400, 531–539, doi:10.1016/j.jmb.2010.05.036.
[69]  Kim, M.; Zhang, Z.; Okano, H.; Yan, D.; Groisman, A.; Hwa, T. Need-based activation of ammonium uptake in Escherichia coli. Mol. Syst. Biol. 2012, 8, 616.
[70]  Yuan, J.; Doucette, C.D.; Fowler, W.U.; Feng, X.-J.; Piazza, M.; Rabitz, H.A.; Wingreen, N.S.; Rabinowitz, J.D. Metabolomics-driven quantitative analysis of ammonia assimilation in E. coli. Mol. Syst. Biol. 2009, 5, 302.
[71]  Commichau, F.M.; Forchhammer, K.; Stulke, J. Regulatory links between carbon and nitrogen metabolism. Curr. Opin. Microbiol. 2006, 9, 167–172, doi:10.1016/j.mib.2006.01.001.
[72]  Mao, X.J.; Huo, Y.X.; Buck, M.; Kolb, A.; Wang, Y.P. Interplay between CRP-cAMP and PII-Ntr systems forms novel regulatory network between carbon metabolism and nitrogen assimilation in Escherichia coli. Nucleic Acids Res. 2007, 35, 1432–1440, doi:10.1093/nar/gkl1142.
[73]  Jiang, P.; Ninfa, A.J. Escherichia coli PII signal transduction protein controlling nitrogen assimilation acts as a sensor of adenylate energy charge in vitro. Biochemistry 2007, 46, 12979–12996.
[74]  Ninfa, J.; Jiang, P. PII signal transduction proteins: Sensors of α-ketoglutarate that regulate nitrogenmetabolism. Curr. Opin. Microbiol. 2005, 8, 168–173, doi:10.1016/j.mib.2005.02.011.
[75]  Hart, Y.; Madar, D.; Yuan, J.; Bren, A; Mayo, A.E.; Rabinowitz, J.D.; Alon, U. Robust control of nitrogen assimilation by a bifunctional enzyme in E. coli. Mol. Cell 2011, 41, 117–127, doi:10.1016/j.molcel.2010.12.023.
[76]  Doucette, C.D.; Schwab, D.J.; Wingreen, N.S.; Rabinowitz, J.D. Alpha-ketoglutarate coordinates carbon and nitrogen utilization via enzyme I inhibition. Nat. Chem. Biol. 2011, 7, 894–901, doi:10.1038/nchembio.685.
[77]  Powell, B.S.; Court, D.L.; Inada, T.; Nakamura, Y.; Michotey, V.; Cui, X.; Reizer, A.; Saier, M.H., Jr.; Reizer, J. Novel proteins of the phosphotransferase system encoded within the rpoN operon of Escherichia coli. Enzyme IIANtr affects growth on organic nitrogen and the conditional lethality of an erats mutant. J. Biol. Chem. 1995, 270, 4822–4839, doi:10.1074/jbc.270.9.4822.
[78]  Peterkofski, A.; Wang, G.; Seok, Y.-J. Parallel PTS systems. Arch. Biochem. Biophys. 2006, 453, 101–107, doi:10.1016/j.abb.2006.01.004.
[79]  Pflüger-Grau, K.; G?rke, B. Regulatory roles of the bacterial nitrogen-related phosphotransferase system. Trend Microbiol. 2010, 18, 205–214, doi:10.1016/j.tim.2010.02.003.
[80]  Lee, C.R.; Cho, S.H.; Yoon, M.J.; Peterkofsky, A.; Seok, Y.J. Escherichia coli enzyme IIANtr regulates the K+ transporter TrkA. Proc. Natl. Acad. Sci. USA 2007, 104, 4124–4129, doi:10.1073/pnas.0609897104.
[81]  Lüttmann, D.; Heermann, R.; Zimmer, B.; Hillmann, A.; Rampp, I.S.; Jung, K.; G?rke, B. Stimulation of the potassium sensor KdpD kinase activity by interaction with the phosphotransferase protein IIANtr in Escherichia coli. Mol. Micobiol. 2009, 72, 978–994, doi:10.1111/j.1365-2958.2009.06704.x.
[82]  Lee, C.-R.; Cho, S.-H.; Kim, H.-J.; Kim, M.; Peterkofsky, A.; Seok, Y.-J. Potassium mediates Escherichia coli enzyme IIANtr-dependent regulation of sigma factor selectivity. Mol. Microbiol. 2010, 78, 1468–1483, doi:10.1111/j.1365-2958.2010.07419.x.
[83]  Lüttmann, D.; G?pel, Y.; G?rke, B. The phosphotransferase protein EIIANtr modulates the phosphate starvation response through interaction with histidine kinase PhoR in Escherichia coli. Mol. Microbiol. 2012, 86, 96–110, doi:10.1111/j.1365-2958.2012.08176.x.
[84]  Kim, H.-J.; Lee, C.-R.; Kim, M.; Peterkofsky, A.; Seok, Y.-J. Dephosphorylated NPr of the nitrogen PTS regulates lipid A biosynthesis by direct interaction with LpxD. Biochem. Biophys. Res. Commun. 2011, 409, 556–561, doi:10.1016/j.bbrc.2011.05.044.
[85]  Lee, C.-R.; Park, Y.-H.; Kim, M.; Kim, Y.-R.; Park, S.; Peterkofsky, A.; Seok, Y.-J. Reciprocal regulation of the autophosphorylation of enzyme INtr by glutamine and α-ketoglutarate in Escherichia coli. Mol. Microbiol. 2013, 88, 473–485, doi:10.1111/mmi.12196.
[86]  Bykowski, T.; van der Ploeg, J.R.; Iwanicka-Nowicka, R.; Hryniewicz, M.M. The switch from inorganic to organic sulphur assimilation in Escherichia coli: Adenosine 5'-phosphosulphate (APS) as a signalling molecule for sulphate excess. Mol. Microbiol. 2002, 43, 1347–1358, doi:10.1046/j.1365-2958.2002.02846.x.
[87]  Kredich, N.M. Biosynthesis of Cysteine. In Escherichia coli and Salmonella: Cellular and Molecular Biology, 2nd ed.; Neidhardt, F.C., Curtiss, R., III, Ingraham, J.L., Lin, E.C.C., Low, K.B., Magasanik, B., Reznikoff, W.S., Riley, M., Schaechter, M., Umbarger, H.H., Eds.; ASM Press: Washington, DC, USA, 1996; Volume 1, pp. 514–527.
[88]  Iwanicka-Nowicka, R.; Hryniewicz, M.M. A new gene, cbl, encoding a member of the LysR family of transcriptional regulators belongs to Escherichia coli cys regulon. Gene 1995, 166, 11–17, doi:10.1016/0378-1119(95)00606-8.
[89]  Zimmer, D.P.; Soupene, H.L.E.; Lee, V.F.; Wendisch, A.B.; Khodursky, B.J.; Peter, R.; Bender, A.; Kustu, S. Nitrogen regulatory protein Ccontrolled genes of Escherichia coli: Scavenging as a defense against nitrogen limitation. Proc. Natl. Acad. Sci. USA 2000, 97, 14674–14679, doi:10.1073/pnas.97.26.14674.
[90]  Gyaneshwar, P.; Paliy, O.; McAuliffe, J.; Popham, D.L.; Jordan, M.I.; Kustu, S. Sulfur and nitrogen limitation in Escherichia coli K-12: Specific homeostatic responses. J. Bacteriol. 2005, 187, 1074–1090, doi:10.1128/JB.187.3.1074-1090.2005.
[91]  Wanner, B.L. Phosphorus Assimilation and Control of the Phosphate Regulon. In Escherichia Coli and Salmonella: Cellular and Molecular Biology; Neidhardt, F.C., Curtiss, R., III, Ingraham, J.L., Eds.; ASM Press: Washington, DC, USA, 1996; pp. 1357–1381.
[92]  Wanner, B.L. Gene regulation by phosphate in enteric bacteria. J. Cell. Biochem. 1993, 51, 47–54, doi:10.1002/jcb.240510110.
[93]  Baek, J.H.; Lee, S.Y. Transcriptome analysis of phosphate starvation response in Escherichia coli. J. Microbiol. Biotechnol. 2007, 17, 244–252.
[94]  Ruiz, N.; Silhavy, T.J. Constitutive activation of the Escherichia coli Pho regulon upregulates rpoS translation in an Hfq dependent fashion. J. Bacteriol. 2003, 185, 5984–5992, doi:10.1128/JB.185.20.5984-5992.2003.
[95]  Taschner, N.P.; Yagil, E.; Spira, B. A differential effect of σs on the expression of the PHO regulon genes of Escherichia coli. Microbiology 2004, 150, 2985–2992, doi:10.1099/mic.0.27124-0.
[96]  Spira, B.; Silberstein, N.; Yagil, E. Guanosine 3',5'-bispyrophosphate (ppGpp) synthesis in cells of Escherichia coli starved for Pi. J. Bacteriol. 1995, 177, 4053–4058.
[97]  Spira, B.; Yagil, E. The integration host factor (IHF) affects the expression of the phosphate-binding protein and of alkaline phosphatase in Escherichia coli. Curr. Microbiol. 1999, 38, 80–85, doi:10.1007/s002849900407.
[98]  Taschner, N.P.; Yagil, E.; Spira, B. The effect of IHF on σs selectivity of the phoA and pst promoters of Escherichia coli. Arch. Microbiol. 2006, 185, 234–237, doi:10.1007/s00203-005-0082-4.
[99]  Schurdell, M.S.; Woodbury, G.M.; McCleary, W.R. Genetic evidence suggests that the intergenic region between pstA and pstB plays a role in the regulation of rpoS translation during phosphate limitation. J. Bacteriol. 2007, 189, 1150–1153, doi:10.1128/JB.01482-06.
[100]  Wanner, B.L.; Wilmes, M.R.; Young, D.C. Control of bacterial alkaline phosphatase synthesis and variation in an Escherichia coli K-12 phoR mutant by adenyl cyclase, the cyclic AMP receptor protein, and the phoM operon. J. Bacteriol. 1988, 170, 1092–1102.
[101]  Kang, Y.; Weber, K.D.; Qiu, Y.; Kiley, P.J.; Blattner, F.R. Genome-wide expression analysis indicates that FNR of Escherichia coli K-12 regulates a large number of genes of unknown function. J. Bacteriol. 2005, 187, 1135–1160, doi:10.1128/JB.187.3.1135-1160.2005.
[102]  Dann, C.E., III; Wakeman, C.A.; Sieling, C.L.; Baker, S.C.; Irnov, I.; Winker, W.C. Structure and mechanism of a metal-sensing regulatory RNA. Cell 2007, 130, 878–892, doi:10.1016/j.cell.2007.06.051.
[103]  Helmann, J.D. Measuring metals with RNA. Mol. Cell. 2007, 27, 859–860, doi:10.1016/j.molcel.2007.09.002.
[104]  Zheng, M.; Doan, B.; Schneider, T.D.; Storz, G. OxyR and SoxRS regulation of fur. J. Biotechnol. 1999, 181, 4639–4643.
[105]  McHugh, J.P.; Rodríguez-Qui?ones, F.; Abdul-Tehrani, H.; Svistunenko, D.A.; Poole, R.K.; Cooper, C.E.; Andrews, S.C. Global iron-dependent gene regulation in Escherichia coli. J. Biol. Chem. 2003, 278, 29478–29486, doi:10.1074/jbc.M303381200.
[106]  Storz, G.; Imlay, J.A. Oxidative stress. Curr. Opin. Microbiol. 1999, 2, 188–194, doi:10.1016/S1369-5274(99)80033-2.
[107]  Gennis, R.B.; Stewart, V. Respiration in Escherichia coli and Salmonella: Cellular and Molecular Biology; Bock, A., Curtiss, R., III, Kaper, J.B., Neidhardt, F.C., Nystrom, T., Rudd, K.E., Squires, C.L., Eds.; ASM Press: Washington, DC, USA, 1996.
[108]  Jovanovic, G.; Lloyde, L.J.; Stumpf, M.P.; Mayhew, A.J.; Buck, M. Induction and function of the phase shock protein extracytoplasmic stress response in Escherichia coli. J. Biol. Chem. 2006, 281, 21147–21161.
[109]  Blanchard, J.R.; Wholey, W.Y.; Conlon, E.M.; Pomposiello, P.J. Rapid changes in gene expression dynamics in response to superoxide reveal SoxRS dependent and independent transcriptional network. PLoS One 2007, 2, e1186, doi:10.1371/journal.pone.0001186.
[110]  Brynildsen, M.P.; Liao, J.C. An integrated network approach indentifies the isobutanol response network of Escherichia coli. Mol. Syst. Biol. 2009, 5, 277.
[111]  Braun, V. Regulation of iron uptake minimizes iron-mediated oxidative stress. J. Biosci. 1998, 23, 483–489, doi:10.1007/BF02936142.
[112]  Azpiroz, M.F.; Lavińa, M. Involvement of enterobactin synthesis pathway in production of Microcin H47. Antimicrob. Agents Chemother. 2004, 48, 1235–1241, doi:10.1128/AAC.48.4.1235-1241.2004.
[113]  Semsey, S.; Andersson, A.M.; Krishna, S.; Jensen, M.H.; Masse, E.; Sneppen, K. Genetic regulation of fluxes: Iron homeostasis of Escherichia coli. Nucleic Acids Res. 2006, 34, 4960–4967, doi:10.1093/nar/gkl627.
[114]  Hantash, F.M.; Ammerlaan, M.; Earhart, C.F. Enterobactin synthase polypeptides of Escherichia coli are present in an osmotic-shocksensitive cytoplasmic locality. Microbiology 1997, 143, 147–156, doi:10.1099/00221287-143-1-147.
[115]  Kumar, R.; Shimizu, K. Transcriptional regulation of main metabolic pathways of cyoA, cydB, fnr, and fur gene knockout Escherichia coli in C-limited and N-limited aerobic continuous cultures. Microb. Cell Fact. 2011, 10, 3, doi:10.1186/1475-2859-10-3.
[116]  Zhang, Z.; Gosset, G.; Barabote, R.; Gonzalez, C.S.; Cuevas, W.A.; Saier, M.H., Jr. Functional interactions between the carbon and iron utilization regulators, Crp and Fur, in Escherichia coli. J. Bacteriol. 2005, 187, 980–990, doi:10.1128/JB.187.3.980-990.2005.
[117]  Ali Azam, T.; Iwata, A.; Nishimura, A.; Ueda, S.; Ishihama, A. Growth phase-dependent variation in protein composition of the Escherichia coli nucleoid. J. Bacteriol. 1999, 181, 6361–6370.
[118]  Bradley, M.D.; Beach, M.B.; de Koning, J.A.P.; Pratt, T.S.; Osuna, R. Effects of Fis on Escherichia coli gene expression during different growth stages. Microbiology 2007, 153, 2922–2940, doi:10.1099/mic.0.2007/008565-0.
[119]  Mallik, P.; Pratt, T.S.; Beach, M.B.; Bradley, M.D.; Undamatla, J.; Osuna, R. Growth phase-dependent regulation and stringent control of fis are conserved processes in enteric bacteria and involve a single promoter (fis P) in Escherichia coli. J. Bacteriol. 2004, 186, 122–135, doi:10.1128/JB.186.1.122-135.2004.
[120]  Mallik, P.; Paul, B.J.; Rutherford, S.T.; Gourse, R.L.; Osuna, R. DksA is required for growth phase-dependent regulation, growth rate-dependent control, and stringent control of fis expression in Escherichia coli. J. Bacteriol. 2006, 188, 5775–5782, doi:10.1128/JB.00276-06.
[121]  Paul, B.J.; Berkmen, M.B.; Gourse, R.L. DksA potentiates direct activation of amino acid promoters by ppGpp. Proc. Natl. Acad. Sci. USA 2005, 102, 7823–7828, doi:10.1073/pnas.0501170102.
[122]  Ferenci, T. Hungry bacteria—definition and properties of a nutritional state. Environ. Microbiol. 2001, 3, 605–611, doi:10.1046/j.1462-2920.2001.00238.x.
[123]  Hardiman, T.; Lemuth, K.; Keller, M.A.; Reuss, M.; Siemann-Herzberg, M. Topology of the global regulatory network of carbon limitation in Escherichia coli. J. Biotechnol. 2007, 132, 359–374, doi:10.1016/j.jbiotec.2007.08.029.
[124]  Braeken, K.; Moris, M.; Daniels, R.; Vanderleyden, J.; Michiels, J. New horizons for (p)ppGpp in bacterial and plant physiology. Trends Microbiol. 2006, 14, 45–54, doi:10.1016/j.tim.2005.11.006.
[125]  Artsimovitch, I.; Patlan, V.; Sekine, S.; Vassylyeva, M.N.; Hosaka, T.; Ochi, K.; Yokoyama, S. Structural basis for transcription regulation by alarmone ppGpp. Cell 2004, 117, 299–310, doi:10.1016/S0092-8674(04)00401-5.
[126]  Kanjee, U.; Ogata, K.; Houry, W.A. Direct binding targets of the stringent response alarmone(p)ppGpp. Mol. Micobiol. 2012, 85, 1029–1043, doi:10.1111/j.1365-2958.2012.08177.x.
[127]  Hengge-Aronis, R. Signal transduction and regulatory mechanisms involved in control of the σs (RpoS) subunit of RNA polymerase. Microbiol. Mol. Biol. Rev. 2002, 66, 373–395, doi:10.1128/MMBR.66.3.373-395.2002.
[128]  Patten, C.L.; Kirchhof, M.G.; Schertzberg, M.R.; Morton, R.A.; Schellhorn, H.E. Microarray analysis of RpoS-mediated gene expression in Escherichia coli K-12. Mol. Genet. Genomics 2004, 272, 580–591, doi:10.1007/s00438-004-1089-2.
[129]  Jishage, M.; Kvint, K.; Shingler, V.; Nystrom, T. Regulation of σfactor competition by the alarmone ppGpp. Genes Dev. 2002, 16, 1260–1270, doi:10.1101/gad.227902.
[130]  Aronis, H.R. Regulation of Gene Expression during Entry into Stationary Phase. In Escherichia Coli and Salmonella: Cellular and Molecular Biology, 2nd ed.; Neidhardt, F.C., Curtiss, R., III, Ingram, J.L., Eds.; ASM Press: Washington, DC, USA, 1996; pp. 1497–1512.
[131]  Aronis, H.R. Stationary phase gene regulation: What makes an Escherichia coli promoter σs-selective? Curr. Opin. Microbiol. 2002, 5, 591–595, doi:10.1016/S1369-5274(02)00372-7.
[132]  Lacour, S.; Landini, P. σs-dependent gene expression at the onset of stationary phase in Escherichia coli: Function of σs-dependent genes and identification of their promoter sequences. J. Bacteriol. 2004, 186, 7186–7195, doi:10.1128/JB.186.21.7186-7195.2004.
[133]  Vijayakumar, S.R.V.; Kirchhof, M.G.; Patten, C.L.; Schellhorn, H.E. RpoS-regulated genes of Escherichia coli identified by random lacZ fusion mutagenesis. J. Bacteriol. 2004, 186, 8499–8507, doi:10.1128/JB.186.24.8499-8507.2004.
[134]  Wei, B.; Shin, S.; LaPorte, D.; Wolfe, A.J.; Romeo, T. Global regulatory mutations in csrA and rpoS cause severe central carbon stress in Escherichia coli in the presence of acetate. J. Bacteriol. 2000, 182, 1632–1640, doi:10.1128/JB.182.6.1632-1640.2000.
[135]  Rahman, M.; Hasan, M.R.; Oba, T.; Shimizu, K. Effect of rpoS gene knockout on the metabolism of Escherichia coli during exponential growth phase and early stationary phase based on gene expressions, enzyme activities and intracellular metabolite concentrations. Biotech. Bioeng. 2006, 94, 585–595, doi:10.1002/bit.20858.
[136]  Weber, H.; Polen, T.; Heuveling, J.; Wendisch, V.F.; Hengge, R. Genome-wide analysis of the general stress response network in Escherichia coli: σs-Dependent genes, promoters, and sigma factor selectivity. J. Bacteriol. 2005, 187, 1591–1603, doi:10.1128/JB.187.5.1591-1603.2005.
[137]  Wang, X.; Dubey, A.K.; Suzuki, K.; Baker, C.S.; Babitzke, P.; Romeo, T. CsrA post-transcriptionally represses pgaABCD, responsible for synthesis of a biofilm polysaccharide adhesin of Escherichia coli. Mol. Microbiol. 2005, 56, 1648–1663, doi:10.1111/j.1365-2958.2005.04648.x.
[138]  Hengge, R. Principles of c-di-GMP signalling in bacteria. Nat. Rev. Microbiol. 2009, 7, 263–273, doi:10.1038/nrmicro2109.
[139]  Barnhart, M.M.; Chapman, M.R. Curli biogenesis and function. Annu. Rev. Microbiol. 2006, 60, 131–147, doi:10.1146/annurev.micro.60.080805.142106.
[140]  Thomason, M.K.; FFontaine, F.; de Lay, N.; Storz1, G. A small RNA that regulates motility and biofilm formation in response to changes in nutrient availability in Escherichia coli. Mol. Microbiol. 2012, 84, 17–35, doi:10.1111/j.1365-2958.2012.07965.x.
[141]  Dong, T.; Schellhorn, H.E. Control of RpoS in global gene expression of Escherichia coli in minimal media. Mol. Genet. Genomics 2009, 281, 19–33, doi:10.1007/s00438-008-0389-3.
[142]  Jackson, D.W.; Simecka, J.W.; Romeo, T. Catabolite repression of Escherichia coli biofilm formation. J. Bacteriol. 2002, 184, 3406–3410, doi:10.1128/JB.184.12.3406-3410.2002.
[143]  Waters, C.M.; Bassler, B.L. Quorum sensing: Cell-to-cell communication in bacteria. Annu. Rev. Cell Dev. Biol. 2005, 21, 319–346, doi:10.1146/annurev.cellbio.21.012704.131001.
[144]  Llorens, N.J.M.; Tormo, A.; Martínez-García, E. Stationary phase in gram-negative bacteria. FEMS Microbiol. Rev. 2010, 34, 476–495, doi:10.1111/j.1574-6976.2010.00213.x.
[145]  Desnues, B.; Cuny, C.; Gregori, G.; Dukan, S.; Aguilaniu, H.; Nystr?m, T. Differential oxidative damage and expression of stress defence regulons in culturable and non-culturable Escherichia coli cells. EMBO Rep. 2003, 4, 400–404, doi:10.1038/sj.embor.embor799.
[146]  Nagamitsu, H.; Murata, M.; Kosaka, T.; Kawaguchi, J.; Mori, H.; Yamada, M. Crucial roles of MicA and RybB as vital factors for σE-dependent cell lysis in Escherichia coli long-term stationary phase. J. Mol. Microbiol. Biotechnol. 2013, 23, 227–232, doi:10.1159/000350370.
[147]  Murata, M.; Noor, R.; Nagamitsu, H.; Tanaka, S.; Yamada, M. Novel pathway directed by sigma E to cause cell lysis in Escherichia coli. Genes Cells 2012, 17, 234–247, doi:10.1111/j.1365-2443.2012.01585.x.
[148]  Noor, R.; Murata, M.; Yamada, M. Oxidative stress as a trigger for growth phase-specific sigmaE-dependent cell lysis in Escherichia coli. J. Mol. Microbiol. Biotechnol. 2009, 17, 177–187, doi:10.1159/000236029.
[149]  Pomposiello, P.J.; Demple, B. Redox-operated genetic switches: The SoxR and OxyR transcription factors. Trends Biotechnol. 2001, 19, 109–114, doi:10.1016/S0167-7799(00)01542-0.
[150]  Gaudu, P.; Weiss, B. SoxR, a [2Fe-2S] transcription factor, is active only in its oxidized form. Proc. Natl. Acad. Sci. USA 1996, 93, 10094–10098, doi:10.1073/pnas.93.19.10094.
[151]  Liochev, S.I.; Fridovich, I. The role of O2. -in the production of HO.: In vitro and in vivo. Free Radic. Biol. Med. 1994, 16, 29–33, doi:10.1016/0891-5849(94)90239-9.
[152]  Greenberg, J.T.; Monach, P.; Chou, J.H.; Josephy, P.D.; Demple, B. Positive control of a global antioxidant defense regulon activated by superoxide-generating agents in Escherichia coli. Proc. Natl. Acad. Sci. USA 1990, 87, 6181–6185, doi:10.1073/pnas.87.16.6181.
[153]  Kabir, M.M.; Shimizu, K. Investigation into the effect of soxR and soxS genes deletion on the central metabolism of Escherichia coli based on gene expressions and enzyme activities. Biochem. Eng. J. 2006, 30, 39–47, doi:10.1016/j.bej.2006.01.015.
[154]  Wolf, R.E.; Prather, D.M.; Shea, F.M. Growth-rate dependent alteration of 6-phosphogluconate dehydrogenase and glucose 6-phosphate dehydrogenase levels in Escherichia coli K-12. J. Bacteriol. 1979, 139, 1093–1096.
[155]  Tsaneva, I.R.; Weiss, B. soxR, a locus governing a superoxide response regulon in Escherichia coli K-12. J. Bacteriol. 1990, 172, 4197–4205.
[156]  Hanson, R.L.; Rose, C. Effects of an insertion mutation in a locus affecting pyridine nucleotide transhydrogenase (pnt::Tn5) on the growth of Escherichia coli. J. Bacteriol. 1980, 141, 401–404.
[157]  Mailloux, R.J.; Bériault, R.; Lemire, J.; Singh, R.; Chénier, R.R.; Hamel, R.D.; Appanna, V.D. The tricarboxylic acid cycle, an ancient metabolic network with a novel twist. PLoS One 2007, 2, e690, doi:10.1371/journal.pone.0000690.
[158]  Johnson, P. Antioxidant enzyme expression in health and disease: Effects of exercise and hypertension. Comp. Biochem. Physiol. C Toxicol. Pharmacol. 2002, 133, 493–505, doi:10.1016/S1532-0456(02)00120-5.
[159]  Foster, J.W. Escherichia coli acid resistance: Tales of an amateur acidophile. Nat. Rev. Microbiol. 2004, 2, 898–907.
[160]  Stincone, A.; Daudi, N.; Rahman, A.S.; Antczak, P.; Henderson, I.; Cole, J.; Johnson, M.D.; Lund, P.; Falciani, F. A systems biology approach sheds new light on Escherichia coli acid resistance. Nucleic Acids Res. 2011, 39, 7512–7528, doi:10.1093/nar/gkr338.
[161]  Richard, H.T.; Foster, J.W. Acid resistance in Escherichia coli. Adv. Appl. Microbiol. 2003, 52, 167–186, doi:10.1016/S0065-2164(03)01007-4.
[162]  Richard, H.T.; Foster, J.W. Escherichia coli glutamate- and arginine- dependent acid resistance systems increase internal pH and reverse transmembrane potential. J. Bacteriol. 2004, 86, 6032–6041, doi:10.1128/JB.186.18.6032-6041.2004.
[163]  Gong, S.; Richard, H.; Foster, J.W. YjdE (AdiC) is the arginine: Agmatine antiporter essential for arginine-dependent acid resistance in Escherichia coli. J. Bacteriol. 2003, 185, 4402–4409, doi:10.1128/JB.185.15.4402-4409.2003.
[164]  Iyer, R.; Williams, C.; Miller, C. Arginin-agmatine antiporter in extreme acid resistance in Escherichia coli. J. Bacteriol. 2003, 185, 6556–6561, doi:10.1128/JB.185.22.6556-6561.2003.
[165]  Castanie-Cornet, M.P.; Foster, J.W. Escherichia coli acid resistance: cAMP receptor protein and a 20 bp cis-acting sequence control pH and stationary phase expression of the gadA and gadBC glutamate decarboxylase genes. Microbiology 2001, 147, 709–715.
[166]  Martin-Galiano, A.J.; Ferrandiz, M.J.; de La Campa, A.G. The promoter of the operon encoding the F0F1 ATPase of Streptococcus pneumonia is inducible by pH. Mol. Microbiol. 2001, 41, 327–338.
[167]  Marzan, L.W.; Shimizu, K. Metabolic regulation of Escherichia coli and its phoB and phoR genes knockout mutants under phosphate and nitrogen limitations as well as at acidic condition. Microb. Cell Fact. 2011, 10, 39, doi:10.1186/1475-2859-10-39.
[168]  Suziedeliene, E.; Suziedelis, K.; Garbenciute, V.; Normark, S. The acid-inducible asr gene in Escherichia coli: Transcriptional control by the phoBR operon. J. Bacteriol. 1999, 181, 2084–2093.
[169]  Kitagawa, M.; Miyakawa, M.; Matsumura, Y.; Tsuchido, T. Escherichia coli small heat shock proteins, IbpA and IbpB, protect enzymes from inactivation by heat and oxidants. Eur. J. Biochem. 2002, 269, 2907–2917, doi:10.1046/j.1432-1033.2002.02958.x.
[170]  S?rensen, H.P.; Mortensen, K.K. Soluble expression of recombinant proteins in the cytoplasm of Escherichia coli. Microb. Cell Fact. 2005, 4, 1, doi:10.1186/1475-2859-4-1.
[171]  Hoffmann, F.; Weber, J.; Rinas, U. Metabolic adaptation of Escherichia coli during temperature-induced recombinant protein production: 1. Readjustment of metabolic enzyme synthesis. Biotechnol. Bioeng. 2002, 80, 313–319, doi:10.1002/bit.10379.
[172]  Tilly, K.; Erickson, J.; Sharma, S.; Georgopoulos, C. Heat shock regulatory gene rpoH mRNA level increases after heat shock in Escherichia coli. J. Bacteriol. 1986, 168, 1155–1158.
[173]  Tilly, K.; Spence, J.; Georgopoulos, C. Modulation of stability of the Escherichia coli heat shock regulatory factor σ32. J. Bacteriol. 1989, 171, 1585–1589.
[174]  Shin, D.; Lim, S.; Seok, Y.J.; Ryu, S. Heat shock RNA polymerase (Eσ32) is involved in the transcription of mlc and Crucial for Induction of the Mlc Regulon by Glucose in Escherichia coli. J. Biol. Chem. 2001, 276, 25871–25875, doi:10.1074/jbc.M101757200.
[175]  Kumari, S.; Beatty, C.M.; Browning, D.F.; Busby, S.J.; Simel, E.J.; Hovel-Miner, G.; Wolfe, A.J. Regulation of acetyl coenzyme A synthetase in Escherichia coli. J. Bacteriol. 2000, 182, 4173–4179, doi:10.1128/JB.182.15.4173-4179.2000.
[176]  Browning, D.F.; Beatty, C.M.; Wolfe, A.J.; Cole, J.A.; Busby, S.J.W. Independent regulation of the divergent Escherichia coli nrfA and acsP1 promoters by a nucleoprotein assembly at a shared regulatory region. Mol. Microbiol. 2002, 43, 687–701, doi:10.1046/j.1365-2958.2002.02776.x.
[177]  Beatty, C.M.; Browning, D.F.; Busby, S.J.W.; Wolfe, A.J. Cyclic AMP receptor protein-dependentactivation of the Escherichia coliacsP2 promoter by a synergistic class III mechanism. J. Bacteriol. 2003, 185, 5148–5157, doi:10.1128/JB.185.17.5148-5157.2003.
[178]  Browning, D.F.; Beatty, C.M.; Sanstad, E.A.; Gunn, K.E.; Busby, S.J.W.; Wolfe, A.J. Modulation of CRP-dependent transcription at the Escherichia coliacsP2 promoter by nucleoprotein complexes: Anti-activation by the nucleoid proteins FIS and IHF. Mol. Microbiol. 2004, 51, 241–254.
[179]  Rahman, M.; Shimizu, K. Altered acetate metabolism and biomass production in several Escherichia coli mutants lacking rpoS-dependent metabolic pathway genes. Mol. Biosyst. 2008, 4, 160–169, doi:10.1039/b712023k.
[180]  Privalle, C.T.; Fridovich, I. Induction of superoxide dismutase in Escherichia coli by heat shock. Proc. Natl. Acad. Sci. USA 1987, 84, 2723–2726, doi:10.1073/pnas.84.9.2723.
[181]  Dunlop, M.J. Engineering microbes for tolerance to next-generation biofuels. Biotechnol. Biofuels. 2011, 4, 32, doi:10.1186/1754-6834-4-32.
[182]  Isken, S.; de Bont, J.A.M. Bacteria tolerant to organic solvents. Extremophiles 1998, 2, 229–238, doi:10.1007/s007920050065.
[183]  Ramos, J.L.; Duque, E.; Gallegos, M.-T.; Godoy, P.; Ramos-Gonzalez, M.I.; Rojas, A.; Teran, W.; Segura, A. Mechanisms of solvent tolerance in Gram-negative bacteria. Annu. Rev. Microbiol. 2002, 56, 743–768, doi:10.1146/annurev.micro.56.012302.161038.
[184]  Nicolaou, S.A.; Gaida, S.M.; Papoutsakis, E.T. A comparative view of metabolite and substrate stress and tolerance in microbial bioprocessing: From biofuels and chemicals, to biocatalysis and bioremediation. Metab. Eng. 2010, 12, 307–331, doi:10.1016/j.ymben.2010.03.004.
[185]  Takatsuka, Y.; Chen, C.; Nikaido, H. Mechanism of recognition of compounds of diverse structures by the multidrug efflux pump AcrB of Escherichia coli. Proc. Natl. Acad. Sci. USA 2010, 107, 6559–6656, doi:10.1073/pnas.1001460107.
[186]  Ankarloo, J.; Wikman, S.; Nicholls, I.A. Escherichia coli mar and acrAB mutants display no tolerance to simple alcohols. Int. J. Mol. Sci. 2010, 11, 1403–1412, doi:10.3390/ijms11041403.
[187]  Piper, P. The heat-shock and ethanol stress responses of yeast exhibit extensive similarity and functional overlap. FEMS Microbiol. Lett. 1995, 134, 121–127, doi:10.1111/j.1574-6968.1995.tb07925.x.
[188]  Rutherford, B.J.; Dahl, R.H.; Price, R.E.; Szmidt, H.L.; Benke, P.I.; Mukhopadhyay, A.; Keasling, J.D. Functional genomic study of exogenous n-butanol stress in Escherichia coli. Appl. Environ. Microbiol. 2010, 76, 1935–1945, doi:10.1128/AEM.02323-09.
[189]  Tomas, C.; Beamish, J.; Papoutsakis, E. Transcriptional analysis of butanol stress and tolerance in Clostridium acetobutylicum. J. Bacteriol. 2004, 186, 2006–2018, doi:10.1128/JB.186.7.2006-2018.2004.
[190]  Fiocco, D.; Capozzi, V.; Goffin, P.; Hols, P.; Spano, G. Improved adaptation to heat, cold, and solvent tolerance in Lactobacillus plantarum. Appl. Microbiol. Biotechnol. 2007, 77, 909–915, doi:10.1007/s00253-007-1228-x.
[191]  Reyes, L.H.; Almario, M.P.; Kao, K.C. Genomic library screens for genes involved in n-butanol tolerance in Escherichia coli. PLoS One 2011, 6, e17678, doi:10.1371/journal.pone.0017678.
[192]  Sikkema, J.; de Bont, J.A.M.; Poolman, B. Mechanisms of membrane toxicity of hydrocarbons. Microbiol. Rev. 1995, 59, 201–222.
[193]  Holtwick, R.; Meinhardt, F.; Keweloh, H. Cis-trans isomerization of unsaturated fatty acids: Cloning and sequencing of the cti gene from Pseudomonas putida P8. Appl. Environ. Microb. 1997, 63, 4292–4297.
[194]  Kiran, M.; Prakash, J.; Annapoorni, S.; Dube, S.; Kusano, T.; Okuyama, H.; Murata, N.; Shivaji, S. Psychrophilic Pseudomonas syringae requires transmonounsaturated fatty acid for growth at higher temperature. Extremophiles 2004, 8, 401–410, doi:10.1007/s00792-004-0401-8.
[195]  Wu, X.; Altman, R.; Eiteman, M.A.; Altman, E. Effect of overexpressing nhaA and nhaR on sodium tolerance and lactate production in Escherichia coli. J. Biol. Eng. 2013, 7, 3, doi:10.1186/1754-1611-7-3.
[196]  Minty, J.J.; Lesnefsky, A.A.; Lin, F.; Chen, Y.; Zaroff, T.A.; Velose, A.B.; Xie, B.; McConnell, C.A.; Ward, R.J.; Schwartz, D.R.; et al. Evolution combined with genomic study elucidates genetic bases of isobutanol tolerance in Escherichia coli. Microb. Cell Fact. 2011, 10, 18, doi:10.1186/1475-2859-10-18.
[197]  Gutierrez-Rios, R.M.; Rosenblueth, D.A.; Loza, J.A.; Huerta, A.M.; Glasner, J.D.; Blattner, F.R.; Collado-Vides, J. Regulatory network of Escherichia coli: Consistency between literature knowledge and microarray profiles. Genome Res. 2003, 13, 2435–2443, doi:10.1101/gr.1387003.
[198]  Maheswaran, M.; Forchhammer, K. Carbon-source-dependent nitrogen regulation in Escherichia coli is mediated through glutamine-dependent GlnB signaling. Microbiology 2003, 149, 2163–2172, doi:10.1099/mic.0.26449-0.
[199]  Quan, J.A.; Schneider, B.L.; Paulsen, I.T.; Yamada, M.; Kredich, N.M.; Saier, M.H., Jr. Regulationof carbon utilization by sulfur availability in Escherichia coli and Salmonella typhimurium. Microbiology 2002, 148, 123–131.
[200]  De Lorenzo, V.; Herrero, M.; Giovannini, F.; Neilands, J.B. Fur (ferric uptake regulation) protein and CAP (catabolite-activator protein) modulate transcription of fur gene in Escherichia coli. Eur. J. Biochem. 1998, 173, 537–546.
[201]  Dragosits, M.; Mozhayskiy, V.; Quinones-Soto, S.; Park, J.; Tagkopoulos, I. Evolutionary potential, cross-stress behavior and the genetic basis of acquired stress resistance in Escherichia coli. Mol. Syst. Biol. 2013, 9, 643.
[202]  Jenkins, D.; Schultz, J.; Matin, A. Starvation-induced cross protection against heat or H2O2 challenge in Escherichia coli. J. Bacteriol. 1988, 170, 3910–3914.
[203]  Jenkins, D.; Auger, E.; Matin, A. Role of RpoH, a heat shock regulator protein, in Escherichia coli carbon starvation protein synthesis and survival. J. Bacteriol. 1991, 173, 1992–1996.
[204]  Gunasekera, T.; Csonka, L.; Paliy, O. Genome-wide transcriptional responses of Escherichia coli K-12 to continuous osmotic and heat stresses. J. Bacteriol. 2008, 190, 3712–3720, doi:10.1128/JB.01990-07.
[205]  White-Ziegler, C.; Um, S.; Pérez, N.; Berns, A.; Malhowski, A.; Young, S. Low temperature (23 degrees C) increases expression of biofilm-, cold-shock- and RpoS-dependent genes in Escherichia coli K-12. Microbiology 2008, 154, 148–166, doi:10.1099/mic.0.2007/012021-0.
[206]  Reaves, M.L.; Rabinowitz, J.D. Metabolomics in systems microbiology Review Article. Curr. Opin. Biotechnol. 2011, 22, 17–25, doi:10.1016/j.copbio.2010.10.001.

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