Literature DB >> 16446111

Pathways of disulfide bond formation in Escherichia coli.

Joris Messens1, Jean-François Collet.   

Abstract

Disulfide bond formation is required for the correct folding of many secreted proteins. Cells possess protein-folding catalysts to ensure that the correct pairs of cysteine residues are joined during the folding process. These enzymatic systems are located in the endoplasmic reticulum of eukaryotes or in the periplasm of Gram-negative bacteria. This review focuses on the pathways of disulfide bond formation and isomerization in bacteria, taking Escherichia coli as a model.

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Year:  2006        PMID： 16446111     DOI： 10.1016/j.biocel.2005.12.011

Source DB:  PubMed          Journal:  Int J Biochem Cell Biol        ISSN： 1357-2725            Impact factor:   5.085


  59 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.  Disulfide bond formation and activation of Escherichia coli β-galactosidase under oxidizing conditions.

Authors:  Joaquin Seras-Franzoso; Roman Affentranger; Mario Ferrer-Navarro; Xavier Daura; Antonio Villaverde; Elena García-Fruitós
Journal:  Appl Environ Microbiol       Date:  2012-01-27       Impact factor: 4.792

3.  Roles of the intramolecular disulfide bridge in MotX and MotY, the specific proteins for sodium-driven motors in Vibrio spp.

Authors:  Jin Yagasaki; Mayuko Okabe; Rie Kurebayashi; Toshiharu Yakushi; Michio Homma
Journal:  J Bacteriol       Date:  2006-07       Impact factor: 3.490

4.  Crystallization and preliminary diffraction analysis of a DsbA homologue from Wolbachia pipientis.

Authors:  M Kurz; I Iturbe-Ormaetxe; R Jarrott; S L O'Neill; K A Byriel; J L Martin; B Heras
Journal:  Acta Crystallogr Sect F Struct Biol Cryst Commun       Date:  2008-01-31

5.  The Escherichia coli CydX protein is a member of the CydAB cytochrome bd oxidase complex and is required for cytochrome bd oxidase activity.

Authors:  Caitlin E VanOrsdel; Shantanu Bhatt; Rondine J Allen; Evan P Brenner; Jessica J Hobson; Aqsa Jamil; Brittany M Haynes; Allyson M Genson; Matthew R Hemm
Journal:  J Bacteriol       Date:  2013-06-07       Impact factor: 3.490

6.  Directed screen of Francisella novicida virulence determinants using Drosophila melanogaster.

Authors:  Monika K Ahlund; Patrik Rydén; Anders Sjöstedt; Svenja Stöven
Journal:  Infect Immun       Date:  2010-05-17       Impact factor: 3.441

7.  A novel component of the disulfide-reducing pathway required for cytochrome c assembly in plastids.

Authors:  Stéphane T Gabilly; Janette Kropat; Mohamed Karamoko; M Dudley Page; Stacie S Nakamoto; Sabeeha S Merchant; Patrice P Hamel
Journal:  Genetics       Date:  2011-01-10       Impact factor: 4.562

Review 8.  Kinetics and mechanisms of thiol-disulfide exchange covering direct substitution and thiol oxidation-mediated pathways.

Authors:  Péter Nagy
Journal:  Antioxid Redox Signal       Date:  2013-01-09       Impact factor: 8.401

9.  Bacterial Periplasmic Oxidoreductases Control the Activity of Oxidized Human Antimicrobial β-Defensin 1.

Authors:  J Wendler; D Ehmann; L Courth; B O Schroeder; N P Malek; J Wehkamp
Journal:  Infect Immun       Date:  2018-03-22       Impact factor: 3.441

10.  Strategies for successful recombinant expression of disulfide bond-dependent proteins in Escherichia coli.

Authors:  Ario de Marco
Journal:  Microb Cell Fact       Date:  2009-05-14       Impact factor: 5.328
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