oalib
Search Results: 1 - 10 of 100 matches for " "
All listed articles are free for downloading (OA Articles)
Page 1 /100
Display every page Item
Cloning and functional characterization of the gene encoding the transcription factor Acel in the basidiomycete Phanerochaete chrysosporium
POLANCO,RUBéN; CANESSA,PAULO; RIVAS,ALEXIS; LARRONDO,LUIS F; LOBOS,SERGIO; VICU?A,RAFAEL;
Biological Research , 2006, DOI: 10.4067/S0716-97602006000500007
Abstract: in this report we describe the isolation and characterization of a gene encoding the transcription factor acel (activation protein of cup 1 expression) in the white rot fungus phanerochaete chrysosporium. pc-acel encodes a predicted protein of 633 amino acids containing the copper-fist dna binding domain typically found in fungal transcription factors such as acel, macl and haal from saccharomyces cerevisiae. the pc-acel gene is localized in scaffold 5, between coordinates 220841 and 222983. a s. cerevisiae acel null mutant strain unable to grow in high-copper medium was fully complemented by transformation with the cdna of pc-acel. moreover, northern blot hybridization studies indicated that pc-acel cdna restores copper inducibility of the yeast cup 1 gene, which encodes the metal-binding protein metallothionein implicated in copper resistance. to our knowledge, this is first report describing an acel transcription factor in basidiomycetes
Cloning and functional characterization of the gene encoding the transcription factor Acel in the basidiomycete Phanerochaete chrysosporium  [cached]
RUBéN POLANCO,PAULO CANESSA,ALEXIS RIVAS,LUIS F LARRONDO
Biological Research , 2006,
Abstract: In this report we describe the isolation and characterization of a gene encoding the transcription factor Acel (Activation protein of cup 1 Expression) in the white rot fungus Phanerochaete chrysosporium. Pc-acel encodes a predicted protein of 633 amino acids containing the copper-fist DNA binding domain typically found in fungal transcription factors such as Acel, Macl and Haal from Saccharomyces cerevisiae. The Pc-acel gene is localized in Scaffold 5, between coordinates 220841 and 222983. A S. cerevisiae acel null mutant strain unable to grow in high-copper medium was fully complemented by transformation with the cDNA of Pc-acel. Moreover, Northern blot hybridization studies indicated that Pc-acel cDNA restores copper inducibility of the yeast cup 1 gene, which encodes the metal-binding protein metallothionein implicated in copper resistance. To our knowledge, this is first report describing an Acel transcription factor in basidiomycetes
Isolation, Molecular Characterization and Reactivity with 2,6 Dichlorophenol of a Laccase and Isolation of Laccase Gene Specific Sequences from Lignin Degrading Basidiomycete Phanerochaete chrysosporium (TL 1)
P.C. Prabu,C. Udayasoorian,G. Balasubramanian
Biotechnology , 2006,
Abstract: A new lignin degrading basidiomycete, Phanerochaete chrysosporium (TL 1) was isolated from pulp and paper mill effluent enriched soil samples can be induced to produce high level laccases when grown on a cellobiose-asparagine liquid medium with 150 μM CuSO4. The fungus grown under static conditions had 70% of total extra cellular laccase protein and about 2.5 fold purification with a final yield of 13.2% of protein purification by Sephadex G-100 column and FPLC. The resultant enzyme pool of the purification process is found to contain a single polypeptide, which produced a single band on an SDS-PAGE. The purified protein showed a specific activity of 106 U mg-1 and the molecular mass (Mr) of native laccase was 65 kDa. The purified laccase has an isoelctric point of 4.0, it is stable in pH range from 4.0 to 6.0 and its optimum pH is 4.5. The optimal reaction temperature is 60°C and stable at 70°C for more than 1 h. Degenerative primers corresponding to the consensus sequences of the copper binding regions in the N-terminal domains of known basidiomycete laccase were used to isolate laccase gene specific sequences from this strain and the laccase gene gave PCR product of about 150 bp and cloned product gave 85% similarity with laccase from T. villosa LCC 2 (L49377).
A calmodulin inhibitor, W-7 influences the effect of cyclic adenosine 3', 5'-monophosphate signaling on ligninolytic enzyme gene expression in Phanerochaete chrysosporium
Takaiku Sakamoto, Yuki Yao, Yoshifumi Hida, Yoichi Honda, Takashi Watanabe, Wataru Hashigaya, Kazumi Suzuki, Toshikazu Irie
AMB Express , 2012, DOI: 10.1186/2191-0855-2-7
Abstract: White-rot fungi are known to have a powerful ligninolytic system that can completely degrade wood lignin (Kirk and Farrell 1987; Kirk et al. 1975) as well as persistent organic pollutants such as dioxin (Bumpus et al. 1985). This ability may be applicable to the construction of a novel potent bioreactor system to convert wood to potent materials and energy sources with low environmental load and to bioremediate polluted environments. However, the ligninolytic property of these fungi is attributable to many known and unknown enzyme genes, expression of which is inductive, and the factors that determine this expression are not completely understood. The lack of knowledge regarding the ligninolytic property of these fungi is an impediment to the development of a highly effective lignin-degrading fungal strain for the construction of an efficient bioreactor system (Cullen and Kersten 2004). The identification of a master regulator that regulates the entire ligninolytic system in white-rot fungi could be used as a target for breeding a high lignin-degrading strain and for furthering our understanding of the lignin-degradation system in these fungi.Phanerochaete chrysosporium, which is the most widely researched white-rot fungus in the world, has 2 families of lignin-degrading peroxidases designated lignin peroxidase (LiP) and manganese peroxidase (MnP) (Heinzkill and Messner 1997). LiP and MnP are thought to play an important role in initiating the lignin degrading reaction of the fungus, because they can cleave lignin structures extracellularly in the first step of lignin mineralization (Cullen and Kersten 2004; Gold et al. 1984; Tien and Kirk 1984). Moreover, LiP and MnP themselves also have potential applications in treating textile effluent (Sedighi et al. 2009; Singh et al. 2010). However, their expression is inductive, related to unknown factors, and known to be unstable, as is the entire ligninolytic system. Information concerning the LiP and MnP expression system
Characterisation of a chimeric Phanerochaete chrysosporium cellobiohydrolase expressed from Escherichia coli
RL Howard, P Masoko, MB Mowa, E Abotsi, S Howard
African Journal of Biotechnology , 2004,
Abstract: The aim of this study was to purify and analyse a Phanerochaete chrysosporium cbhI.1 gene-product expressed as an inducible, secreted, heterologous protein from an Escerichia coli pGEXcbhI.1 clone. Using glutathione Sepharose 4B affinity chromatography, the expressed protein was purified from the supernatant of an induced E. coli transformed with pGEXcbhI.1 and ran as a single band on a Sodium dodecyl sulphate-polyacrylamide gel. The glutathione S-transferase (GST) fused CBHI.1 was approx-imately 80 kDa in size, approximately 2.2 kDa smaller than the theoretically predicted size. The purified protein exhibited time dependent hydrolytic reaction against carboxy-methyl-cellulose (CMC) and Avicel. On CMC the highest hydrolytic reaction occurred at 120 min. whereas for Avicel it was at 150 min. Optimum pH and temperature for activity of the protein against these cellulose substrates were pH 6 and 55oC, respectively, and the protein remained stable under these optimum conditions for 24 h. Key Words: Phanerochaete chrysosporium, cellobiohydrolase purification, heterologus expression. African Journal of Biotechnology Vol.3(7) 2004: 349-352
Isolation and Characterization of Promoters from Phanerochaete chrysosporium
黄孢原毛平革菌基因启动子的分离与鉴定

LI Wei,ZHANG Yi-Zheng,
李维
,张义正

生物工程学报 , 2000,
Abstract: Promoter-probe vector pSUPV8 was used to clone promoters from Phanerochaete chrysosporium directly in Escherichia coli. Six hygromycin B-resistant recombinants were obtained and two inserted fragments of them were sequenced. The results indicated that they contain several sequences similar to eukaryotic cis regulatory elements. Only pCH6 could transform P, chrysosporium into hygromecin B resistance. PCR and dot hybridization analysis indicated that it was introduced into P. chrysosporium successfully and leaded to the HmB-resistance. The results demonstrated that HmB-resistant gene (hph) could be used as an ideal reporter gene for P. chrysosporium transformation.
Molecular cloning and expression of alcohol dehydrogenase gene of Phanerochaete chrysosporium
黄孢原毛平革菌乙醇脱氢酶基因的克隆和表达

HE Chuan,WU Jin-Ming,ZHANG Xi-Gen,WU Bo,ZHANG Yi-Zheng,
何川
,吴近名,张希根,吴波,张义正

遗传 , 2009,
Abstract: 乙醇是黄孢原毛平革菌(Phanerochaete chrysosporium)在限氧培养条件下重要的代谢物之一,为了更好的理解P.chrysosporium在低氧条件下的代谢机制,文章从P.chrysosporium中克隆到一个长1071 bp的乙醇脱氢酶基因PCAdhl cDNA.该基因编码一个由356个氨基酸组成的蛋白质,它与其他生物的乙醇脱氢酶的氨基酸序列的相似性很低,但酶催化活性位点序列却高度保守.将PCAdhl在大肠杆菌中表达,并获得有酶活性的重组蛋白.纯化的蛋白质用于制备抗体.半定量RT-PCR和Western blot分析结果显示,在限氧条件的培养过程中,PCAdhl基因在mRNA水平和蛋白水平上都保持相对稳定,表明该基因的表达是组成型的;但从菌丝体提取的粗蛋白中的乙醇脱氢酶活性却随着培养时间的增加及氧气含量的持续降低而逐渐升高,这暗示P.chrysospo-rium中存在其他低氧诱导型乙醇脱氢酶基因的表达.
ADSORPTION OF CONGO RED DYE ON HAZELNUT SHELLS AND DEGRADATION WITH Phanerochaete chrysosporium  [PDF]
Riccardo A. Carletto,Fabiana Chimirri,Francesca Bosco,Franco Ferrero
BioResources , 2008,
Abstract: The present work concerns the experimental evaluation of hazelnut shells as a low cost natural biosorbent. Adsorption of the direct azo dye Congo Red was performed within a concentrations range of 50-5000 mg/L. Hazelnut shells were employed as organic support for Phanerochaete chrysosporium cultures to study the best cultural medium composition for the MnP production. The capability of Phanerochaete chrysosporium to take macronutrients as carbon and nitrogen from hazelnut shells was demonstrated. Cultures of Phanerochaete chrysosporium were carried out with hazelnut shells coming from Congo Red adsorption tests, showing that 43% of the adsorbed dye was degraded.
Effect of nitrogen concentration in culture mediums on growth and enzyme production of Phanerochaete chrysosporium
GAO Da-wen,WEN Xiang-hua,QIAN Yi,
GAO Da-wen
,WEN Xiang-hu,QIAN Yi

环境科学学报(英文版) , 2005,
Abstract: Effect of different nitrogen concentration in the mediums on growth and enzyme production of Phanerochaete chrysosporium was studied when glucose concentration was 10 g/L. The results showed that the medium contained 0.8 g/L ammonium tartrate is the best. It not only supply abundant nutrients for the growth of Phanerochaete chrysosporium, which make mycelia the best grow compared with the other medium, but also produce higher manganese-dependent peroxidase (Mnp) and laccase (Lac) activity. In addition, it is observed that the variation of mycelia surface is related to ligninolytic enzyme secreted by Phanerochaete chrysosporium. When the surface of mycelium pellets appeared burs, it predicts secondary metabolism begin. This experimentation demonstrated that when the ratio of carbon and nitrogen in nitrogen limited medium is equal to 100:8, growth and enzyme production of Phanerochaete chrysosporium is the best, it could achieve the maximum Mnp and Lac activity.
Expression of lignin peroxidase H2 from Phanerochaete chrysosporium by multi-copy recombinant Pichia strain

WANG Wei,WEN Xianghua,

环境科学学报(英文版) , 2009,
Abstract: The lipH2 gene, encoding the expression of lignin peroxidase, was cloned from Phanerochaete chrysosporium BKM-F-1767 and expressed in Pichia pastoris X-33, a yeast.The cDNA of LiPH2 was generated from total RNA extracted from P.chrysosporium by PCR with primers that do not contain a P.chrysosporium lignin peroxidase secretion signal.The gene was then successfully inserted into the expression vector pPICZα, resulting in the recombinant vector pPICZα-lipH2.The transformation was conducted in two ways.One was using the wild Pichia pastoris as the recipients, which results in the recombinant P.pastoris with single or low lipH2 gene copy.The second was using P.pastoris and single or low lipH2 gene copy as the recipients, which results in the recombinant P.pastoris with multi-copies of lipH2 genes.This study first expressed the gene lipH2 in P.pastoris and achieved the successful expression of the LiPH2 depending upon the generation of a recombinant strain that contains multiple copies.The lignin peroxidase activity reached a maximum of 15 U/L after 12 h induction.
Page 1 /100
Display every page Item


Home
Copyright © 2008-2017 Open Access Library. All rights reserved.