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PMID: 20367276 Published · ppublish English Journal Article Research Support, N.I.H., Extramural Research Support, Non-U.S. Gov't Review

Mechanisms of oxidative protein folding in the bacterial cell envelope.

Antioxidants & redox signaling ·Vol. 13 ·No. 8 ·2010-10-00 ·Pages 1231-46

Kadokura H, Beckwith J

Abstract

Disulfide-bond formation is important for the correct folding of a great number of proteins that are exported to the cell envelope of bacteria. Bacterial cells have evolved elaborate systems to promote the joining of two cysteines to form a disulfide bond and to repair misoxidized proteins. In the past two decades, significant advances have occurred in our understanding of the enzyme systems (DsbA, DsbB, DsbC, DsbG, and DsbD) used by the gram-negative bacterium Escherichia coli to ensure that correct pairs of cysteines are joined during the process of protein folding. However, a number of fundamental questions about these processes remain, especially about how they occur inside the cell. In addition, recent recognition of the increasing diversity among bacteria in the disulfide bond-forming capacity and in the systems for introducing disulfide bonds into proteins is raising new questions. We review here the marked progress in this field and discuss important questions that remain for future studies.

MeSH Terms
Cell Membrane/metabolism Disulfides/metabolism Escherichia coli/cytology,metabolism Escherichia coli Proteins/chemistry,metabolism Oxidation-Reduction Protein Folding
Chemicals
Disulfides Escherichia coli Proteins
Authors & Affiliations
2 authors, click to expand affiliations / ORCID
Kadokura Hiroshi
Graduate School of Biological Sciences, Nara Institute of Science and Technology, Takayama, Ikoma, Nara, Japan. hkadokura@bs.naist.jp
Beckwith Jon
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Article Info
Journal
Antioxidants & redox signaling
Abbr.
Antioxid Redox Signal
ISSN
1557-7716
DOI
10.1089/ars.2010.3187
Email
hkadokura@bs.naist.jp
Published
2010-10-00
Pages
1231-46
Language
English
Region
United States
NLM ID
100888899
PMCID
PMC2959184
Subset
IM
Grants
NIGMS NIH HHS · R01 GM041883 · United States
NIGMS NIH HHS · GM41883 · United States
External Links
PubMed source DOI: 10.1089/ars.2010.3187 PMC Full Text View journal details
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