Literature DB >> 18342631

Disulfide bond isomerization in prokaryotes.

Stefan Gleiter1, James C A Bardwell.   

Abstract

Proteins with multiple cysteine residues often require disulfide isomerization reactions before they attain their correct conformation. In prokaryotes this reaction is catalyzed mainly by DsbC, a protein that shares many similarities in structure and mechanism to the eukaryotic protein disulfide isomerase. This review discusses the current knowledge about disulfide isomerization in prokaryotes.

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Year:  2008        PMID： 18342631      PMCID： PMC2391271          DOI： 10.1016/j.bbamcr.2008.02.009

Source DB:  PubMed          Journal:  Biochim Biophys Acta        ISSN： 0006-3002


  44 in total

1.  DsbG, a protein disulfide isomerase with chaperone activity.

Authors:  F Shao; M W Bader; U Jakob; J C Bardwell
Journal:  J Biol Chem       Date:  2000-05-05       Impact factor: 5.157

2.  Oxidative protein folding is driven by the electron transport system.

Authors:  M Bader; W Muse; D P Ballou; C Gassner; J C Bardwell
Journal:  Cell       Date:  1999-07-23       Impact factor: 41.582

3.  Contributions of substrate binding to the catalytic activity of DsbC.

Authors:  N J Darby; S Raina; T E Creighton
Journal:  Biochemistry       Date:  1998-01-20       Impact factor: 3.162

4.  Disulfide bonds are generated by quinone reduction.

Authors:  M W Bader; T Xie; C A Yu; J C Bardwell
Journal:  J Biol Chem       Date:  2000-08-25       Impact factor: 5.157

5.  Respiratory chain strongly oxidizes the CXXC motif of DsbB in the Escherichia coli disulfide bond formation pathway.

Authors:  T Kobayashi; K Ito
Journal:  EMBO J       Date:  1999-03-01       Impact factor: 11.598

6.  The reactive and destabilizing disulfide bond of DsbA, a protein required for protein disulfide bond formation in vivo.

Authors:  A Zapun; J C Bardwell; T E Creighton
Journal:  Biochemistry       Date:  1993-05-18       Impact factor: 3.162

7.  DsbA and DsbC-catalyzed oxidative folding of proteins with complex disulfide bridge patterns in vitro and in vivo.

Authors:  Klaus Maskos; Martina Huber-Wunderlich; Rudi Glockshuber
Journal:  J Mol Biol       Date:  2003-01-17       Impact factor: 5.469

8.  Structural and functional characterization of DsbC, a protein involved in disulfide bond formation in Escherichia coli.

Authors:  A Zapun; D Missiakas; S Raina; T E Creighton
Journal:  Biochemistry       Date:  1995-04-18       Impact factor: 3.162

9.  Identification and characterization of a new disulfide isomerase-like protein (DsbD) in Escherichia coli.

Authors:  D Missiakas; F Schwager; S Raina
Journal:  EMBO J       Date:  1995-07-17       Impact factor: 11.598

10.  Characterization of DsbC, a periplasmic protein of Erwinia chrysanthemi and Escherichia coli with disulfide isomerase activity.

Authors:  V E Shevchik; G Condemine; J Robert-Baudouy
Journal:  EMBO J       Date:  1994-04-15       Impact factor: 11.598
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  26 in total

1.  The protein-disulfide isomerase DsbC cooperates with SurA and DsbA in the assembly of the essential β-barrel protein LptD.

Authors:  Katleen Denoncin; Didier Vertommen; Eunok Paek; Jean-François Collet
Journal:  J Biol Chem       Date:  2010-07-07       Impact factor: 5.157

2.  Role of dimerization in the catalytic properties of the Escherichia coli disulfide isomerase DsbC.

Authors:  Silvia A Arredondo; Tiffany F Chen; Austen F Riggs; Hiram F Gilbert; George Georgiou
Journal:  J Biol Chem       Date:  2009-07-06       Impact factor: 5.157

3.  Enhancing protein stability with extended disulfide bonds.

Authors:  Tao Liu; Yan Wang; Xiaozhou Luo; Jack Li; Sean A Reed; Han Xiao; Travis S Young; Peter G Schultz
Journal:  Proc Natl Acad Sci U S A       Date:  2016-05-09       Impact factor: 11.205

4.  Thiol redox requirements and substrate specificities of recombinant cytochrome c assembly systems II and III.

Authors:  Cynthia L Richard-Fogal; Brian San Francisco; Elaine R Frawley; Robert G Kranz
Journal:  Biochim Biophys Acta       Date:  2011-09-16

5.  Co-expression of Dsb proteins enables soluble expression of a single-chain variable fragment (scFv) against human type 1 insulin-like growth factor receptor (IGF-1R) in E. coli.

Authors:  Xue-Wen Sun; Xiao-Hua Wang; Yan-Bing Yao
Journal:  World J Microbiol Biotechnol       Date:  2014-09-26       Impact factor: 3.312

6.  Conformational rearrangements in the N-domain of Escherichia coli FepA during ferric enterobactin transport.

Authors:  Aritri Majumdar; Vy Trinh; Kyle J Moore; Chuck R Smallwood; Ashish Kumar; Taihao Yang; Daniel C Scott; Noah J Long; Salete M Newton; Phillip E Klebba
Journal:  J Biol Chem       Date:  2020-02-25       Impact factor: 5.157

7.  Difference gel electrophoresis identifies differentially expressed proteins in endoscopically collected pancreatic fluid.

Authors:  Joao A Paulo; Linda S Lee; Peter A Banks; Hanno Steen; Darwin L Conwell
Journal:  Electrophoresis       Date:  2011-08       Impact factor: 3.535

8.  Engineered pathways for correct disulfide bond oxidation.

Authors:  Guoping Ren; James C A Bardwell
Journal:  Antioxid Redox Signal       Date:  2011-03-31       Impact factor: 8.401

9.  Chaperone domains convert prolyl isomerases into generic catalysts of protein folding.

Authors:  Roman P Jakob; Gabriel Zoldák; Tobias Aumüller; Franz X Schmid
Journal:  Proc Natl Acad Sci U S A       Date:  2009-11-17       Impact factor: 11.205

Review 10.  Ribosomal peptide natural products: bridging the ribosomal and nonribosomal worlds.

Authors:  John A McIntosh; Mohamed S Donia; Eric W Schmidt
Journal:  Nat Prod Rep       Date:  2009-04       Impact factor: 13.423
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