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Search Results: 1 - 10 of 325627 matches for " Leda S. Chubatsu "
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Comparative molecular analysis of Herbaspirillum strains by RAPD, RFLP, and 16S rDNA sequencing
Soares-Ramos Juliana R.L.,Ramos Humberto J.O.,Cruz Leonardo M.,Chubatsu Leda S.
Genetics and Molecular Biology , 2003,
Abstract: Herbaspirillum spp. are endophytic diazotrophic bacteria associated with important agricultural crops. In this work, we analyzed six strains of H. seropedicae (Z78, M2, ZA69, ZA95, Z152, and Z67) and one strain of H. rubrisubalbicans (M4) by restriction fragment length polymorphism (RFLP) using HindIII or DraI restriction endonucleases, random amplified polymorphic DNA (RAPD), and partial sequencing of 16S rDNA. The results of these analyses ascribed the strains studied to three distinct groups: group I, consisting of M2 and M4; group II, of ZA69; and group III, of ZA95, Z78, Z67, and Z152. RAPD fingerprinting showed a higher variability than the other methods, and each strain had a unique electrophoretic pattern with five of the six primers used. Interestingly, H. seropedicae M2 was found by all analyses to be genetically very close to H. rubrisubalbicans M4. Our results show that RAPD can distinguish between all Herbaspirillum strains tested.
Identification and characterization of PhbF: A DNA binding protein with regulatory role in the PHB metabolism of Herbaspirillum seropedicae SmR1
Marco AS Kadowaki, Marcelo Müller-Santos, Fabiane GM Rego, Emanuel M Souza, Marshall G Yates, Rose A Monteiro, Fabio O Pedrosa, Leda S Chubatsu, Maria BR Steffens
BMC Microbiology , 2011, DOI: 10.1186/1471-2180-11-230
Abstract: In this work we describe the characterization of the PhbF protein from H. seropedicae SmR1 which was purified and characterized after expression in E. coli. The purified PhbF protein was able to bind to eleven putative promoters of genes involved in PHB metabolism in H. seropedicae SmR1. In silico analyses indicated a probable DNA-binding sequence which was shown to be protected in DNA footprinting assays using purified PhbF. Analyses using lacZ fusions showed that PhbF can act as a repressor protein controlling the expression of PHB metabolism-related genes.Our results indicate that H. seropedicae SmR1 PhbF regulates expression of phb-related genes by acting as a transcriptional repressor. The knowledge of the PHB metabolism of this plant-associated bacterium may contribute to the understanding of the plant-colonizing process and the organism's resistance and survival in planta.Polyhydroxyalkanoates (PHA) are aliphatic polyesters biosynthesized by several bacteria [1-4] as a means of carbon storage and a source of reducing equivalents when other nutrients are limiting. The most frequently PHA produced is poly(3-hydroxybutyrate) or PHB [2]. The ability to produce PHB has been correlated with improved survival under stress conditions or in competitive environments [5,6]. PHB is generally produced in conditions of carbon oversupply and low levels of other nutrients such as nitrogen, phosphate or oxygen [7]. The biosynthesis of PHB is dependent on the activity of the following enzymes: (i) a 3-ketothiolase which condenses two acetyl-CoA yielding acetoacetyl-CoA (encoded by phbA), (ii) a NADPH-dependent acetoacetyl-CoA reductase which reduces acetoacetyl-CoA to (R)-3-hydroxybutyryl-CoA (encoded by phbB) and (iii) the PHB synthase (encoded by phbC) that catalyses the polymerization of (R)-3-hydroxybutyryl-CoA to form the polymer [8,9]. This polymer is stored intracellularly as insoluble inclusion bodies called PHB granules [1] which also contain about 2% protein as well
Role of PII proteins in nitrogen fixation control of Herbaspirillum seropedicae strain SmR1
Lilian Noindorf, Ana C Bonatto, Rose A Monteiro, Emanuel M Souza, Liu U Rigo, Fabio O Pedrosa, Maria BR Steffens, Leda S Chubatsu
BMC Microbiology , 2011, DOI: 10.1186/1471-2180-11-8
Abstract: In order to determine the involvement of the H. seropedicae glnB and glnK gene products in nitrogen fixation, a series of mutant strains were constructed and characterized. The glnK- mutants were deficient in nitrogen fixation and they were complemented by plasmids expressing the GlnK protein or an N-truncated form of NifA. The nitrogenase post-translational control by ammonium was studied and the results showed that the glnK mutant is partially defective in nitrogenase inactivation upon addition of ammonium while the glnB mutant has a wild-type phenotype.Our results indicate that GlnK is mainly responsible for NifA activity regulation and ammonium-dependent post-translational regulation of nitrogenase in H. seropedicae.The PII family comprises homotrimeric proteins that have important roles in the control of the central metabolism in bacteria and plants, acting as transducers of the cellular nitrogen and carbon levels [1,2]. In many Proteobacteria studied there is a pair of PII proteins, usually called GlnB and GlnK, and their function is to sense the cellular levels of nitrogen, carbon and energy by binding the effectors 2-oxoglutarate, ATP and ADP [2,3]. These signals are then relayed to target proteins through conformational changes triggered by interaction with the effectors. The proteobacterial PII proteins also undergo a cycle of uridylylation/deuridylylation catalyzed by the bifunctional GlnD protein [1] in response to the intracellular levels of nitrogen. These conformational and covalent state changes stimulate or inhibit interactions of PII with different cellular protein targets involved in nitrogen and carbon metabolism [2].PII proteins are key players in the regulation of nitrogen fixation in Proteobacteria. In Klebsiella pneumoniae and Azotobacter vinelandii, GlnK is required to regulate the activity of NifL, which inhibits NifA, the nif gene specific activator, under nitrogen-excess conditions [4-6]. In Azospirillum brasilense and Rhodospirillum rubr
Comparative molecular analysis of Herbaspirillum strains by RAPD, RFLP, and 16S rDNA sequencing
Soares-Ramos, Juliana R.L.;Ramos, Humberto J.O.;Cruz, Leonardo M.;Chubatsu, Leda S.;Pedrosa, Fábio O.;Rigo, Liu U.;Souza, Emanuel M.;
Genetics and Molecular Biology , 2003, DOI: 10.1590/S1415-47572003000400019
Abstract: herbaspirillum spp. are endophytic diazotrophic bacteria associated with important agricultural crops. in this work, we analyzed six strains of h. seropedicae (z78, m2, za69, za95, z152, and z67) and one strain of h. rubrisubalbicans (m4) by restriction fragment length polymorphism (rflp) using hindiii or drai restriction endonucleases, random amplified polymorphic dna (rapd), and partial sequencing of 16s rdna. the results of these analyses ascribed the strains studied to three distinct groups: group i, consisting of m2 and m4; group ii, of za69; and group iii, of za95, z78, z67, and z152. rapd fingerprinting showed a higher variability than the other methods, and each strain had a unique electrophoretic pattern with five of the six primers used. interestingly, h. seropedicae m2 was found by all analyses to be genetically very close to h. rubrisubalbicans m4. our results show that rapd can distinguish between all herbaspirillum strains tested.
Expression, purification and DNA-binding activities of two putative ModE proteins of Herbaspirillum seropedicae (Burkholderiales, Oxalobacteraceae)
Souza, André L.F.;Chubatsu, Leda S.;Souza, Emanuel M.;Pedrosa, Fábio O.;Monteiro, Rose A.;Rego, Fabiane G.M.;Rigo, Liu U.;
Genetics and Molecular Biology , 2008, DOI: 10.1590/S1415-47572008000400022
Abstract: in prokaryotes molybdenum is taken up by a high-affinity abc-type transporter system encoded by the modabc genes. the endophyte β-proteobacterium herbaspirillum seropedicae has two modabc gene clusters and two genes encoding putative mo-dependent regulator proteins (mode1 and mode2). analysis of the amino acid sequence of the mode1 protein of h. seropedicae revealed the presence of an n-terminal domain containing a dna-binding helix-turn-helix motif (hth) and a c-terminal domain with a molybdate-binding motif. the second putative regulator protein, mode2, contains only the helix-turn-helix motif, similar to that observed in some sequenced genomes. we cloned the mode1 (810 bp) and mode2 (372 bp) genes and expressed them in escherichia coli as his-tagged fusion proteins, which we subsequently purified. the over-expressed recombinant his-mode1 was insoluble and was purified after solubilization with urea and then on-column refolded during affinity chromatography. the his-mode2 was expressed as a soluble protein and purified by affinity chromatography. these purified proteins were analyzed by dna band-shift assays using the moda2 promoter region as probe. our results indicate that his-mode1 and his-mode2 are able to bind to the moda2 promoter region, suggesting that both proteins may play a role in the regulation of molybdenum uptake and metabolism in h. seropedicae.
Identification of Proteins Associated with Polyhydroxybutyrate Granules from Herbaspirillum seropedicae SmR1 - Old Partners, New Players
Evandro F. Tirapelle, Marcelo Müller-Santos, Michelle Z. Tadra-Sfeir, Marco A. S. Kadowaki, Maria B. R. Steffens, Rose A. Monteiro, Emanuel M. Souza, Fabio O. Pedrosa, Leda S. Chubatsu
PLOS ONE , 2013, DOI: 10.1371/journal.pone.0075066
Abstract: Herbaspirillum seropedicae is a diazotrophic ?-Proteobacterium found associated with important agricultural crops. This bacterium produces polyhydroxybutyrate (PHB), an aliphatic polyester, as a carbon storage and/or source of reducing equivalents. The PHB polymer is stored as intracellular insoluble granules coated mainly with proteins, some of which are directly involved in PHB synthesis, degradation and granule biogenesis. In this work, we have extracted the PHB granules from H. seropedicae and identified their associated-proteins by mass spectrometry. This analysis allowed us to identify the main phasin (PhaP1) coating the PHB granule as well as the PHB synthase (PhbC1) responsible for its synthesis. A phbC1 mutant is impaired in PHB synthesis, confirming its role in H. seropedicae. On the other hand, a phaP1 mutant produces PHB granules but coated mainly with the secondary phasin (PhaP2). Furthermore, some novel proteins not previously described to be involved with PHB metabolism were also identified, bringing new possibilities to PHB function in H. seropedicae.
Maize Root Lectins Mediate the Interaction with Herbaspirillum seropedicae via N-Acetyl Glucosamine Residues of Lipopolysaccharides
Eduardo Balsanelli, Thalita Regina Tuleski, Valter Antonio de Baura, Marshall Geoffrey Yates, Leda Satie Chubatsu, Fabio de Oliveira Pedrosa, Emanuel Maltempi de Souza, Rose Adele Monteiro
PLOS ONE , 2013, DOI: 10.1371/journal.pone.0077001
Abstract: Herbaspirillum seropedicae is a plant growth-promoting diazotrophic betaproteobacterium which associates with important crops, such as maize, wheat, rice and sugar-cane. We have previously reported that intact lipopolysaccharide (LPS) is required for H. seropedicae attachment and endophytic colonization of maize roots. In this study, we present evidence that the LPS biosynthesis gene waaL (codes for the O-antigen ligase) is induced during rhizosphere colonization by H. seropedicae. Furthermore a waaL mutant strain lacking the O-antigen portion of the LPS is severely impaired in colonization. Since N-acetyl glucosamine inhibits H. seropedicae attachment to maize roots, lectin-like proteins from maize roots (MRLs) were isolated and mass spectrometry (MS) analysis showed that MRL-1 and MRL-2 correspond to maize proteins with a jacalin-like lectin domain, while MRL-3 contains a B-chain lectin domain. These proteins showed agglutination activity against wild type H. seropedicae, but failed to agglutinate the waaL mutant strain. The agglutination reaction was severely diminished in the presence of N-acetyl glucosamine. Moreover addition of the MRL proteins as competitors in H. seropedicae attachment assays decreased 80-fold the adhesion of the wild type to maize roots. The results suggest that N-acetyl glucosamine residues of the LPS O-antigen bind to maize root lectins, an essential step for efficient bacterial attachment and colonization.
Genome of Herbaspirillum seropedicae Strain SmR1, a Specialized Diazotrophic Endophyte of Tropical Grasses
Fábio O. Pedrosa ,Rose Adele Monteiro,Roseli Wassem,Leonardo M. Cruz,Ricardo A. Ayub,Nelson B. Colauto,Maria Aparecida Fernandez,Maria Helena P. Fungaro,Edmundo C. Grisard,Mariangela Hungria,Humberto M. F. Madeira,Rubens O. Nodari,Clarice A. Osaku,Maria Luiza Petzl-Erler,Hernán Terenzi,Luiz G. E. Vieira,Maria Berenice R. Steffens,Vinicius A. Weiss,Luiz F. P. Pereira,Marina I. M. Almeida,Lysangela R. Alves,Anelis Marin,Luiza Maria Araujo,Eduardo Balsanelli,Valter A. Baura,Leda S. Chubatsu,Helisson Faoro,Augusto Favetti,Geraldo Friedermann,Chirlei Glienke,Susan Karp,Vanessa Kava-Cordeiro,Roberto T. Raittz,Humberto J. O. Ramos,Enilze Maria S. F. Ribeiro,Liu Un Rigo,Saul N. Rocha,Stefan Schwab,Anilda G. Silva,Eliel M. Souza,Michelle Z. Tadra-Sfeir,Rodrigo A. Torres,Audrei N. G. Dabul,Maria Albertina M. Soares,Luciano S. Gasques,Ciela C. T. Gimenes,Juliana S. Valle,Ricardo R. Ciferri,Luiz C. Correa,Norma K. Murace,Jo?o A. Pamphile,Eliana Valéria Patussi,Alberto J. Prioli,Sonia Maria A. Prioli,Carmem Lúcia M. S. C. Rocha,Olívia Márcia N. Arantes,Márcia Cristina Furlaneto,Leandro P. Godoy,Carlos E. C. Oliveira,Daniele Satori,Laurival A. Vilas-Boas,Maria Angélica E. Watanabe,Bibiana Paula Dambros,Miguel P. Guerra,Sandra Marisa Mathioni,Karine Louise Santos,Mario Steindel,Javier Vernal,Fernando G. Barcellos,Rubens J. Campo,Ligia Maria O. Chueire,Marisa Fabiana Nicolás,Lilian Pereira-Ferrari,José L. da Concei??o Silva,Nereida M. R. Gioppo,Vladimir P. Margarido
PLOS Genetics , 2011, DOI: 10.1371/journal.pgen.1002064
Abstract: The molecular mechanisms of plant recognition, colonization, and nutrient exchange between diazotrophic endophytes and plants are scarcely known. Herbaspirillum seropedicae is an endophytic bacterium capable of colonizing intercellular spaces of grasses such as rice and sugar cane. The genome of H. seropedicae strain SmR1 was sequenced and annotated by The Paraná State Genome Programme—GENOPAR. The genome is composed of a circular chromosome of 5,513,887 bp and contains a total of 4,804 genes. The genome sequence revealed that H. seropedicae is a highly versatile microorganism with capacity to metabolize a wide range of carbon and nitrogen sources and with possession of four distinct terminal oxidases. The genome contains a multitude of protein secretion systems, including type I, type II, type III, type V, and type VI secretion systems, and type IV pili, suggesting a high potential to interact with host plants. H. seropedicae is able to synthesize indole acetic acid as reflected by the four IAA biosynthetic pathways present. A gene coding for ACC deaminase, which may be involved in modulating the associated plant ethylene-signaling pathway, is also present. Genes for hemagglutinins/hemolysins/adhesins were found and may play a role in plant cell surface adhesion. These features may endow H. seropedicae with the ability to establish an endophytic life-style in a large number of plant species.
Sexualidade de puérperas com bebês de risco
Belentani, Leda Maria;Marcon, S?nia Silva;Pelloso, Sandra Marisa;
Acta Paulista de Enfermagem , 2011, DOI: 10.1590/S0103-21002011000100016
Abstract: objective: to identify possible changes in the sexuality patterns of women who have high-risk infants in the first six months postpartum. methods: a cohort study of 193 mothers of high-risk infants born between may and october of 2008, who were included in the newborn risk surveillance program in maringá (paraná, brasil). data were collected through semi-structured interviews during two home visits (at 45 days and six months postpartum). results: among these participants, 45.8% and 26.3% indicated that their sexuality patterns were worse than before pregnancy at 45 days and six months after delivery, respectively. there was no association between sexuality patterns and any variable at 45 days; at six months post-delivery, associations with complications in pregnancy (p = 0.0259) and living with a partner (p = 0.0093) were identified. conclusion: mothers of high-risk infants, especially those who experienced complications during pregnancy, require multidisciplinary, long-term monitoring of sexuality patterns
Analysis of genetic variability in three species of Pimelodidae (Ostariophysi - Siluriformes)
Almeida, Fernanda S. de;Sodré, Leda M.K.;
Genetics and Molecular Biology , 1998, DOI: 10.1590/S1415-47571998000400014
Abstract: genetic variability of three pimelodidae species, pimelodus maculatus, iheringichthys labrosus, and pinirampus pirinampu, collected at one site in the tibagi river, was comparatively analyzed using protein data for six systems which code 15 loci in liver, muscle, and heart. the proportion of polymorphic loci () for p. maculatus, i. labrosus, and p. pirinampu was 13.33, 20, and 6.67%, respectively, and mean heterozigosity was 6, 8.3, and 4.3%. the genetic identity value (i) was 0.32 between p. maculatus and i. labrosus, 0.37 between p. maculatus and p. pirinampu, and 0.58 between i. labrosus and p. pirinampu. this value suggests that these two latter species are congeneric. however, morphological characteristics place these species in distinct genera.
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