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Genomes and Genes | dsbASummaryGene Symbol: dsbA Description: periplasmic protein disulfide isomerase I Alias: ECK3852, JW3832, dsf, iarA, ppfA Species: Top Publications
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Publications
The DsbA signal sequence directs efficient, cotranslational export of passenger proteins to the Escherichia coli periplasm via the signal recognition particle pathwayClark F Schierle
Department of Microbiology and Molecular Genetics, Harvard Medical School, Boston, Massachusetts 02115, USA
J Bacteriol 185:5706-13. 2003..protein thioredoxin 1 can be efficiently exported to the periplasmic space by the signal sequence of the DsbA protein (DsbAss) but not by the signal sequence of alkaline phosphatase (PhoA) or maltose binding protein (MBP)...- In vivo substrate specificity of periplasmic disulfide oxidoreductasesAnnie Hiniker
Program in Cellular and Molecular Biology, University of Michigan, 830 N University, Ann Arbor, MI 48109 1048, USA
J Biol Chem 279:12967-73. 2004..coli periplasmic disulfide oxidoreductases, including the well characterized oxidase DsbA, has not yet been performed... - Building bridges: disulphide bond formation in the cellJ C Bardwell
Institut fur Biophysik und Physikalische Biochemie, Universitat Regensburg, Germany
Mol Microbiol 14:199-205. 1994..Disulphide bond formation in Escherichia coli is catalysed by at least three 'Dsb' proteins; DsbA, -B and -C... - A selection for mutants that interfere with folding of Escherichia coli thioredoxin-1 in vivoDamon Huber
Department of Microbiology and Molecular Genetics, Harvard Medical School, Boston, MA 02115, USA
Proc Natl Acad Sci U S A 102:18872-7. 2005..When exported to the periplasm, it can partially replace the activity of DsbA in promoting the formation of disulfide bonds... - Identification of a protein required for disulfide bond formation in vivoJ C Bardwell
Department of Microbiology and Molecular Genetics, Harvard Medical School, Boston, Massachusetts 02115
Cell 67:581-9. 1991We describe a mutation (dsbA) that renders Escherichia coli severely defective in disulfide bond formation. In dsbA mutant cells, pulse-labeled beta-lactamase, alkaline phosphatase, and OmpA are secreted but largely lack disulfide bonds... - Snapshots of DsbA in action: detection of proteins in the process of oxidative foldingHiroshi Kadokura
Department of Microbiology and Molecular Genetics, Harvard Medical School, Boston, MA 02115, USA
Science 303:534-7. 2004b>DsbA, a thioredoxin superfamily member, introduces disulfide bonds into newly translocated proteins. This process is thought to occur via formation of mixed disulfide complexes between DsbA and its substrates... - Engineered DsbC chimeras catalyze both protein oxidation and disulfide-bond isomerization in Escherichia coli: Reconciling two competing pathwaysLaura Segatori
Department of Chemical Engineering, University of Texas, Austin, 78712, USA
Proc Natl Acad Sci U S A 101:10018-23. 2004In the Escherichia coli periplasm, the formation of protein disulfide bonds is catalyzed by DsbA and DsbC... - Characterization of the menaquinone-dependent disulfide bond formation pathway of Escherichia coliYoh hei Takahashi
Institute for Virus Research, Kyoto University, Sakyo ku, Kyoto 606 8507, Japan
J Biol Chem 279:47057-65. 2004..In the protein disulfide-introducing system of Escherichia coli, plasma membrane-integrated DsbB oxidizes periplasmic DsbA, the primary disulfide donor... - Structure of circularly permuted DsbA(Q100T99): preserved global fold and local structural adjustmentsBabu A Manjasetty
Forschungsgruppe Kristallographie, Max Delbruck Centrum fur Molekulare Medizin, D 13092 Berlin, Germany
Acta Crystallogr D Biol Crystallogr 60:304-9. 2004The thiol-disulfide oxidoreductase DsbA is required for efficient formation of disulfide bonds in the Escherichia coli periplasm... - The unusual transmembrane electron transporter DsbD and its homologues: a bacterial family of disulfide reductasesAmir Porat
Department of Microbiology and Molecular Genetics, Harvard Medical School, 200 Longwood Avenue, Boston, MA 02115, USA
Res Microbiol 155:617-22. 2004..Its substrates include protein disulfide isomerases and a protein involved in cytochrome c assembly. Two membrane-embedded cysteines in DsbD alternate between the disulfide-bonded (oxidized) and reduced states in this process... - Disulfide bond formation system in Escherichia coliKenji Inaba
Division of Protein Chemistry, Post Genome Science Center, Medical Institute of Bioregulation, Kyushu University, 3 1 1 Maidashi, Higashi ku, Fukuoka 812 8582, Japan
J Biochem 146:591-7. 2009..Coexisting in the periplasm of Escherichia coli are the DsbA-DsbB disulfide-introducing and DsbC-DsbD disulfide-isomerizing pathways, which promote the oxidative folding of .. - DsbB elicits a red-shift of bound ubiquinone during the catalysis of DsbA oxidationKenji Inaba
Institute for Virus Research, Kyoto University, Kyoto 606 8507, Japan
J Biol Chem 279:6761-8. 2004DsbB is an Escherichia coli plasma membrane protein that reoxidizes the Cys30-Pro-His-Cys33 active site of DsbA, the primary dithiol oxidant in the periplasm... - A cytochrome b562 variant with a c-type cytochrome CXXCH heme-binding motif as a probe of the Escherichia coli cytochrome c maturation systemJames W A Allen
Department of Biochemistry, University of Oxford, South Parks Road, Oxford OX1 3QU, United Kingdom
J Biol Chem 278:52075-83. 2003..coli strains deficient in the periplasmic reductant DsbD or oxidant DsbA. In the DsbA- strain under aerobic conditions, c-type cytochromes were made abundantly and correctly when the Ccm .. - Mechanism of the electron transfer catalyst DsbB from Escherichia coliUlla Grauschopf
Institut fur Molekularbiologie und Biophysik, Eidgenossische Technische Hochschule Honggerberg, CH 8093 Zurich, Switzerland
EMBO J 22:3503-13. 2003..coli is essential for disulfide bond formation and catalyses the oxidation of the periplasmic dithiol oxidase DsbA by ubiquinone. DsbB contains two catalytic disulfide bonds, Cys41-Cys44 and Cys104-Cys130... - Role of the Escherichia coli Tat pathway in outer membrane integrityBérengère Ize
Department of Molecular Microbiology, John Innes Centre, Norwich NR4 7UH, UK
Mol Microbiol 48:1183-93. 2003..The presence of genes encoding amidases with twin-arginine signal sequences in the genomes of other Gram-negative bacteria suggests that a similar cell envelope defect may be a common feature of tat mutant strains... - Disulfide bond isomerization in prokaryotesAnnie Hiniker
Medical Scientist Training Program, University of Michigan Medical School, Ann Arbor, Michigan 48109, USA
Biochemistry 42:1179-85. 2003 - [Redox properties and conformational changes of DsbA protein from Escherichia coli periplasm]Qi Li
Institute of Biochemistry and Cell Biology, Shanghai Institutes for Biological Sciences, The Chinese Academy of Sciences, Shanghai 200031, China
Sheng Wu Hua Xue Yu Sheng Wu Wu Li Xue Bao (Shanghai) 34:583-8. 2002b>DsbA protein, a disulfide bond enzyme in Escherichia coli periplasm, catalyzes mainly disulfide bond formation of proteins... - Protein thiol modifications visualized in vivoLars I Leichert
Department of Molecular, Cellular, and Developmental Biology, University of Michigan, Ann Arbor, Michigan, USA
PLoS Biol 2:e333. 2004..thiols were periplasmic proteins and were found to be in vivo substrates of the disulfide-bond-forming protein DsbA. We discovered a substantial number of redox-sensitive cytoplasmic proteins, whose thiol groups were significantly .. - Key players involved in bacterial disulfide-bond formationJacqueline T Tan
Department of Molecular, Cellular, and Developmental Biology, University of Michigan, 830 North University, Ann Arbor, MI 48109, USA
Chembiochem 5:1479-87. 2004 - Mutational analysis of the disulfide catalysts DsbA and DsbBJacqueline Tan
Department of Molecular and Cellular Developmental Biology, University of Michigan, Ann Arbor, MI 48109, USA
J Bacteriol 187:1504-10. 2005In prokaryotes, disulfides are generated by the DsbA-DsbB system. DsbB functions to generate disulfides by quinone reduction. These disulfides are passed to the DsbA protein and then to folding proteins... - Preparation and structure of the charge-transfer intermediate of the transmembrane redox catalyst DsbBGoran Malojcic
ETH Zurich, Institute of Molecular Biology and Biophysics, CH 8093 Zurich, Switzerland
FEBS Lett 582:3301-7. 2008..In bacteria, disulfide bonds are introduced by the periplasmic dithiol oxidase DsbA, which transfers its catalytic disulfide bond to folding polypeptides... - Bacterial species exhibit diversity in their mechanisms and capacity for protein disulfide bond formationRachel J Dutton
Department of Microbiology and Molecular Genetics, Harvard Medical School, 200 Longwood Avenue, Boston, MA 02115, USA
Proc Natl Acad Sci U S A 105:11933-8. 2008.... - SRP and Sec pathway leader peptides for antibody phage display and antibody fragment production in E. coliHolger Thie
Technische Universitat Braunschweig, Institut für Biochemie und Biotechnologie, Abteilung Biotechnologie, Spielmannstr 7, 38106 Braunschweig, Germany
N Biotechnol 25:49-54. 2008..Four leader peptides using the Sec pathway (PelB, OmpA, PhoA and pIII) and three using the SRP pathway (DsbA, TorT and TolB) were compared... - Mutants in DsbB that appear to redirect oxidation through the disulfide isomerization pathwayJonathan L Pan
Howard Hughes Medical Institute, University of Michigan, Ann Arbor, MI 48109, USA
J Mol Biol 377:1433-42. 2008Disulfide bond formation occurs in secreted proteins in Escherichia coli when the disulfide oxidoreductase DsbA, a soluble periplasmic protein, nonspecifically transfers a disulfide to a substrate protein... - Modeling Escherichia coli signal peptidase complex with bound substrate: determinants in the mature peptide influencing signal peptide cleavageKhar Heng Choo
Institute for Infocomm Research, 21 Heng Mui Keng Terrace, Singapore 119613
BMC Bioinformatics 9:S15. 2008..We report here a structure-based model for Escherichia coli DsbA 13-25 in complex with its endogenous type I SPase. - The role of disulfide bond isomerase A (DsbA) of Escherichia coli O157:H7 in biofilm formation and virulenceYunho Lee
FEMS Microbiol Lett 278:213-22. 2008The role of periplasmic disulfide oxidoreductase DsbA in Shiga toxin-producing Escherichia coli O157:H7 (STEC) was investigated. Deletion of dsbA (DeltadsbA) significantly decreased cell motility and alkaline phosphatase activity in STEC... - A bacterial two-hybrid system based on the twin-arginine transporter pathway of E. coliEva Maria Strauch
Department of Chemistry and Biochemistry, University of Texas, Austin, Texas 78712, USA
Protein Sci 16:1001-8. 2007..In addition, we introduce the use of the cysteine disulfide oxidase DsbA as a reporter... - Kinetic characterization of the disulfide bond-forming enzyme DsbBTimothy L Tapley
Department of Molecular, Cellular and Developmental Biology, University of Michigan, Ann Arbor Michigan 48109, USA
J Biol Chem 282:10263-71. 2007..In the process of transferring electrons from DsbA to a tightly bound ubiquinone cofactor, DsbB undergoes an unusual spectral transition at approximately 510 nm... - Characterization of disulfide exchange between DsbA and HtrA proteins from Escherichia coliJoanna Skorko-Glonek
Department of Biochemistry, University of Gdansk, Gdansk, Poland
Acta Biochim Pol 53:585-9. 2006b>DsbA is the major oxidase responsible for generation of disulfide bonds in proteins of E. coli envelope... - [Periplasmatic disulfide oxidoreductases from bacterium Escherichia coli--their structure and function]Joanna Skórko-Glónekv
Department of Biochemistry, Insitute of Biology, University of Gdansk, 24 Kladki St, 80 822 Gdansk, Poland
Postepy Biochem 51:459-67. 2005..These proteins function in two separate pathways: (1) oxidizing (DsbA/DsbB system), responsible for introducing S-S bonds, and (2) reducing (DsbC/DsbD system, DsbG, CcmG and CcmH) which .. - Copper stress causes an in vivo requirement for the Escherichia coli disulfide isomerase DsbCAnnie Hiniker
Program in Cellular and Molecular Biology, University of Michigan, 48109 1048, USA
J Biol Chem 280:33785-91. 2005In Escherichia coli, the periplasmic disulfide oxidoreductase DsbA is thought to be a powerful but nonspecific oxidant, joining cysteines together the moment they enter the periplasm... - Detecting folding intermediates of a protein as it passes through the bacterial translocation channelHiroshi Kadokura
Department of Microbiology and Molecular Genetics, Harvard Medical School, Boston, MA 02115, USA
Cell 138:1164-73. 2009..cotranslational and posttranslational folding intermediates of a periplasmic protein in which the protein and DsbA, a periplasmic disulfide bond-forming enzyme, are covalently linked by a disulfide bond... - Peculiar properties of DsbA in its export across the Escherichia coli cytoplasmic membraneNobuyuki Shimohata
Institute for Virus Research, Kyoto University, Kyoto 606 8507, Japan
J Bacteriol 187:3997-4004. 2005Export of DsbA, a protein disulfide bond-introducing enzyme, across the Escherichia coli cytoplasmic membrane was studied with special reference to the effects of various mutations affecting translocation factors... - Randomization of the entire active-site helix alpha 1 of the thiol-disulfide oxidoreductase DsbA from Escherichia coliBjorn Philipps
Institut fur Molekularbiologie und Biophysik, Eidgenossische Technische Hochschule Honggerberg, CH 8093 Zurich, Switzerland
J Biol Chem 277:43050-7. 2002b>DsbA from Escherichia coli is the most oxidizing member of the thiol-disulfide oxidoreductase family (E(o)' = -122 mV) and is required for efficient disulfide bond formation in the periplasm... - Paradoxical redox properties of DsbB and DsbA in the protein disulfide-introducing reaction cascadeKenji Inaba
Institute for Virus Research, Japan Science and Technology Corporation, Kyoto University, Kyoto 606 8507, Japan
EMBO J 21:2646-54. 2002..redox properties of the redox active sites in DsbB to gain further insights into the catalytic mechanisms of DsbA oxidation. The standard redox potential of DsbB was determined to be -0... - Oxidative protein folding in bacteriaJean Francois Collet
Department of Molecular, Cellular and Developmental Biology, University of Michigan, Ann Arbor, MI 48109 1048, USA
Mol Microbiol 44:1-8. 2002..Disulphide bonds are donated directly to unfolded polypeptides by the DsbA protein; DsbA is reoxidized by DsbB. DsbB generates disulphides de novo from oxidized quinones... - A mutation in the dsbA gene coding for periplasmic disulfide oxidoreductase reduces transcription of the Escherichia coli ompF geneA P Pugsley
Unité de Génétique Moléculaire CNRS URA 1149, Institut Pasteur, Paris, France
Mol Gen Genet 237:407-11. 1993An insertion mutation in the Escherichia coli dsbA gene, coding for periplasmic disulfide oxidoreductase, dramatically reduces the level of OmpF porin protein in the cell envelope... - A pathway for disulfide bond formation in vivoJ C Bardwell
Department of Microbiology and Molecular Genetics, Harvard Medical School, Boston, MA 02115
Proc Natl Acad Sci U S A 90:1038-42. 1993Protein disulfide bond formation in Escherichia coli requires the periplasmic protein DsbA. We describe here mutations in the gene for a second protein, DsbB, which is also necessary for disulfide bond formation... - Crystal structure of the DsbA protein required for disulphide bond formation in vivoJ L Martin
Rockefeller University, New York, New York
Nature 365:464-8. 1993..The folding of such proteins is greatly accelerated in Escherichia coli by DsbA, but the mechanism of this rate enhancement is not well understood... - The redox properties of protein disulfide isomerase (DsbA) of Escherichia coli result from a tense conformation of its oxidized formM Wunderlich
Institut fur Biophysik und Physikalische Biochemie, Universitat Regensburg, Germany
J Mol Biol 233:559-66. 1993Periplasmic protein disulfide isomerase (DsbA) from Escherichia coli is a strongly oxidizing thiol reagent with one catalytic disulfide bridge and an intrinsic redox potential of -0.089 V... - A pleîotropic acid phosphatase-deficient mutant of Escherichia coli shows premature termination in the dsbA gene. Use of dsbA::phoA fusions to localize a structurally important domain in DsbAP Belin
Departement d Ingenierie et d Etudes des Proteines, C E SACLAY, CEA, Gif sur Yvette, France
Mol Gen Genet 242:23-32. 1994..A DNA fragment that complements the mutation was cloned and shown to carry the dsbA gene, which encodes a periplasmic disulphide bond-forming factor... - Bacterial protein disulfide isomerase: efficient catalysis of oxidative protein folding at acidic pHM Wunderlich
Institut fur Biophysik und Physikalische Biochemie, Universitat Regensburg, Germany
Biochemistry 32:12251-6. 1993Periplasmic protein disulfide isomerase (DsbA) is essential for disulfide formation in Escherichia coli... - Reactivity and ionization of the active site cysteine residues of DsbA, a protein required for disulfide bond formation in vivoJ W Nelson
European Molecular Biology Laboratory, Heidelberg, Germany
Biochemistry 33:5974-83. 1994b>DsbA is a periplasmic protein of Escherichia coli that appears to be the immediate donor of disulfide bonds to proteins that are secreted... - PapD chaperone function in pilus biogenesis depends on oxidant and chaperone-like activities of DsbAF Jacob-Dubuisson
Department of Molecular Microbiology, Washington University Medical School, St Louis, MO 63110 1093
Proc Natl Acad Sci U S A 91:11552-6. 1994..of uropathogenic Escherichia coli were not assembled by a strain that lacks the periplasmic disulfide isomerase DsbA. This defect was mostly attributed to the immunoglobulin-like pilus chaperone PapD, which possesses an unusual .. - A mutation in either dsbA or dsbB, a gene encoding a component of a periplasmic disulfide bond-catalyzing system, is required for high-level expression of the Bacteroides fragilis metallo-beta-lactamase, CcrA, in Escherichia coliL E Alksne
Department of Molecular Biology, American Cyanamid Company, Pearl River, New York 10965
J Bacteriol 177:462-4. 1995..Bacteroides fragilis is functionally expressed in Escherichia coli only in the presence of a genomic mutation in iarA or iarB (increased ampicillin resistance), identified in this study as dsbA or dsbB, respectively... - Evidence that the pathway of disulfide bond formation in Escherichia coli involves interactions between the cysteines of DsbB and DsbAC Guilhot
Department of Microbiology and Molecular Genetics, Harvard Medical School, Boston, MA 02115, USA
Proc Natl Acad Sci U S A 92:9895-9. 1995..This process involves at least two proteins: DsbA and DsbB... - An essential role for DsbA in cytochrome c synthesis and formate-dependent nitrite reduction by Escherichia coli K-12R Metheringham
School of Biochemistry, University of Birmingham, UK
Arch Microbiol 164:301-7. 1995..The mutation was localized by conjugation, transduction, and Southern blotting experiments to the dsbA gene at minute 87 on the E. coli chromosome and was complemented by the wild-type allele... - Translocation of a folded protein across the outer membrane in Escherichia coliA P Pugsley
Unité de Génétique Moléculaire, Centre National de la Recherche Scientifique URA1149, Institut Pasteur, Paris, France
Proc Natl Acad Sci U S A 89:12058-62. 1992A mutation in the Escherichia coli dsbA gene (coding for a periplasmic disulfide oxidoreductase) reduces the rate of disulfide bond formation in the enzyme pullulanase and also reduces the rate at which the enzyme is secreted to the cell .. - Mutants in disulfide bond formation that disrupt flagellar assembly in Escherichia coliF E Dailey
Department of Cellular and Developmental Biology, Harvard University, Cambridge, MA 02138
Proc Natl Acad Sci U S A 90:1043-7. 1993..Cystine suppresses this defect in dsbB strains. We also show that dsbA strains [Bardwell, J. C. A., McGovern, K. & Beckwith, J... - The reactive and destabilizing disulfide bond of DsbA, a protein required for protein disulfide bond formation in vivoA Zapun
European Molecular Biology Labortory, Heidelberg, Germany
Biochemistry 32:5083-92. 1993The protein DsbA facilitates disulfide bond formation in the periplasm of Escherichia coli. It has only two cysteine residues that are separated in the sequence by two other residues and are shown to form a disulfide bond reversibly... - A mutant hunt for defects in membrane protein assembly yields mutations affecting the bacterial signal recognition particle and Sec machineryH Tian
Department of Microbiology and Molecular Genetics, Harvard Medical School, 200 Longwood Avenue, Boston, MA 02115, USA
Proc Natl Acad Sci U S A 97:4730-5. 2000..The mutants defective in disulfide bond formation include additional classes of dsbA and dsbB mutations... - Identification of Tn10 insertions in the dsbA gene affecting Escherichia coli biofilm formationP Genevaux
Department of Molecular Microbiology, Faculty of Biology, Free University of Amsterdam, The Netherlands
FEMS Microbiol Lett 173:403-9. 1999..Three adhesion mutants harbored the transposon in the dsbA gene, whose product, DsbA, catalyses folding of numerous extracytoplasmic disulfide bond-containing proteins... - On the functional interchangeability, oxidant versus reductant, of members of the thioredoxin superfamilyL Debarbieux
Department of Microbiology and Molecular Genetics, Harvard Medical School, Boston, Massachusetts 02115, USA
J Bacteriol 182:723-7. 2000..where it can also act as an oxidant, replacing the normal periplasmic catalyst of disulfide bond formation, DsbA, in oxidizing cell envelope proteins (L. Debarbieux and J. Beckwith, Proc. Natl. Acad. Sci... - Mutagenic studies on human protein disulfide isomerase by complementation of Escherichia coli dsbA and dsbC mutantsS J Stafford
School of Biosciences, University of Birmingham, Edgbaston, UK
FEBS Lett 466:317-22. 2000..two simple in vivo assays for these activities of PDI, based on the demonstration that PDI can complement both a dsbA mutation and a dsbC mutation when expressed to the periplasm of Escherichia coli... - Crystal structures of reduced and oxidized DsbA: investigation of domain motion and thiolate stabilizationL W Guddat
Centre for Drug Design and Development University of Queensland Brisbane, QLD, 4072, Australia
Structure 6:757-67. 1998..The bacterial protein-folding factor DsbA is the most oxidizing of the thioredoxin family... - Disulfide bond catalysts in Escherichia coliT Zander
Department of Biology, University of Michigan, Ann Arbor 48109, USA
Methods Enzymol 290:59-74. 1998 - Oversynthesis of a new Escherichia coli small RNA suppresses export toxicity of DsbA'-PhoA unfoldable periplasmic proteinsA Guigueno
Departement d Ingenierie et d Etudes des Proteines, Commissariat a l Energie Atomique, 91191 Gif sur Yvette, France
J Bacteriol 183:1147-58. 2001In Escherichia coli, the DsbA'-PhoA hybrid proteins carrying an unfoldable DsbA' fragment can be targeted to the envelope, where they exert their toxicity... - The uncharged surface features surrounding the active site of Escherichia coli DsbA are conserved and are implicated in peptide bindingL W Guddat
Centre for Drug Design and Development, University of Queensland, Brisbane, Australia
Protein Sci 6:1148-56. 1997b>DsbA is a protein-folding catalyst from the periplasm of Escherichia coli that interacts with newly translocated polypeptide substrate and catalyzes the formation of disulfide bonds in these secreted proteins... - Catalysis of disulfide bond formation and isomerization in Escherichia coliM W Bader
Department of Molecular Cellular and Developmental Biology, University of Michigan, Ann Arbor, Michigan 48109-1048, USA
Adv Protein Chem 59:283-301. 2001 - Regulation of Escherichia coli cell envelope proteins involved in protein folding and degradation by the Cpx two-component systemJ Pogliano
Department of Microbiology and Molecular Genetics, Harvard Medical School, Boston, Massachusetts 02115, USA
Genes Dev 11:1169-82. 1997..First, activation of the Cpx pathway induces 5- to 10-fold the synthesis of DsbA, required for disulfide bond formation, and DegP, a major periplasmic protease... - Roles of cysteine residues of DsbB in its activity to reoxidize DsbA, the protein disulphide bond catalyst of Escherichia coliS Kishigami
Department of Cell Biology, Institute for Virus Research, Kyoto University, Japan
Genes Cells 1:201-8. 1996b>DsbA, a periplasmic protein, catalyses the disulphide bond formation of other cell surface proteins in E. coli... - Mutations in dsbA and dsbB, but not dsbC, lead to an enhanced sensitivity of Escherichia coli to Hg2+ and Cd2+S J Stafford
School of Biological Sciences, University of Birmingham, Edgbaston, UK
FEMS Microbiol Lett 174:179-84. 1999..Mutations in dsbA or dsbB, but not dsbC, increase the proportion of proteins with free thiols in the periplasm compared to wild-type... - Generation of monoclonal antibodies against Escherichia coli DsbAYuan Zhang
Department of Immunology, Fourth Military Medical University, Xi an Shaanxi Province, PR China
Hybridoma (Larchmt) 27:131-4. 2008Disulfide oxidoreductase A (also known as disulfide bond formation protein A, or DsbA) is produced in Escherichia coli (E... - Evidence for proton shuffling in a thioredoxin-like protein during catalysisDaniele Narzi
Theoretical and Computational Membrane Biology, Center for Bioinformatics, Saarland University, Box 15 11 50, D 66041 Saarbrucken, Germany
J Mol Biol 382:978-86. 2008..A consistent catalytic mechanism for DsbL, probably conferrable to other proteins of the same class, is presented. Our results suggest a functional role of hydration entropy of active-site groups... - Identification and characterization of an Escherichia coli gene required for the formation of correctly folded alkaline phosphatase, a periplasmic enzymeS Kamitani
Department of Cell Biology, Kyoto University, Japan
EMBO J 11:57-62. 1992..It was susceptible to degradation by proteases in vivo and in vitro. The wild-type counterpart of this gene (named ppfA) has been sequenced and shown to encode a periplasmic protein with a pair of potentially redox-active cysteine .. - In vitro catalysis of oxidative folding of disulfide-bonded proteins by the Escherichia coli dsbA (ppfA) gene productY Akiyama
Institute for Virus Research, Kyoto University, Japan
J Biol Chem 267:22440-5. 1992It was shown previously that the Escherichia coli gene ppfA (dsbA) encodes a periplasmic protein, and its inactivation leads to a deficiency in disulfide bond formation of envelope proteins (Kamitani, S., Akiyama, Y., and Ito, K... - The disulphide isomerase DsbC cooperates with the oxidase DsbA in a DsbD-independent mannerDidier Vertommen
de Duve Institute, Universite Catholique de Louvain, B 1200 Brussels, Belgium
Mol Microbiol 67:336-49. 2008In Escherichia coli, DsbA introduces disulphide bonds into secreted proteins. DsbA is recycled by DsbB, which generates disulphides from quinone reduction... - Maturation pathway of Escherichia coli heat-stable enterotoxin I: requirement of DsbA for disulfide bond formationH Yamanaka
Department of Biochemistry, Faculty of Pharmaceutical Sciences, Tokushima Bunri University, Japan
J Bacteriol 176:2906-13. 1994..The involvement of DsbA in the formation of the disulfide bonds of STp was examined in this study... - Crystal structure of the DsbB-DsbA complex reveals a mechanism of disulfide bond generationKenji Inaba
Institute for Virus Research, Kyoto University and CREST, Japan Science and Technology Agency, Kyoto 606 8507, Japan
Cell 127:789-801. 2006..DsbB is an E. coli membrane protein that oxidizes DsbA, a periplasmic dithiol oxidase... - Structural analysis of three His32 mutants of DsbA: support for an electrostatic role of His32 in DsbA stabilityL W Guddat
Centre for Drug Design and Development, University of Queensland, Brisbane, Australia
Protein Sci 6:1893-900. 1997b>DsbA, a 21-kDa protein from Escherichia coli, is a potent oxidizing disulfide catalyst required for disulfide bond formation in secreted proteins... - The sigma(E) and the Cpx signal transduction systems control the synthesis of periplasmic protein-folding enzymes in Escherichia coliP N Danese
Department of Molecular Biology, Princeton University, New Jersey 08544, USA
Genes Dev 11:1183-93. 1997..Similarly, the Cpx system controls transcription of the dsbA locus, which encodes a periplasmic enzyme required for efficient disulfide bond formation in several .. - Reactivities of quinone-free DsbB from Escherichia coliKenji Inaba
Institute for Virus Research, Kyoto University, and CREST of Japan Science and Technology Agency, Kyoto 606 8507, Japan
J Biol Chem 280:33035-44. 2005..and Cys104-Cys130, facing the periplasm, as well as the bound quinone molecules play crucial roles in oxidizing DsbA, the protein dithiol oxidant in the periplasm...