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Oxidative protein folding in bacteria
dc.contributor.authorCollet, Jean-Francoisen_US
dc.contributor.authorBardwell, James C. A.en_US
dc.date.accessioned2010-06-01T22:07:42Z
dc.date.available2010-06-01T22:07:42Z
dc.date.issued2002-04en_US
dc.identifier.citationCollet, Jean-Francois; Bardwell, James C. A. (2002). "Oxidative protein folding in bacteria." Molecular Microbiology 44(1): 1-8. <http://hdl.handle.net/2027.42/75150>en_US
dc.identifier.issn0950-382Xen_US
dc.identifier.issn1365-2958en_US
dc.identifier.urihttps://hdl.handle.net/2027.42/75150
dc.identifier.urihttp://www.ncbi.nlm.nih.gov/sites/entrez?cmd=retrieve&db=pubmed&list_uids=11967064&dopt=citationen_US
dc.description.abstractTen years ago it was thought that disulphide bond formation in prokaryotes occurred spontaneously. Now two pathways involved in disulphide bond formation have been well characterized, the oxidative pathway, which is responsible for the formation of disulphides, and the isomerization pathway, which shuffles incorrectly formed disulphides. 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. These quinones are reoxidized by the electron transport chain, showing that disulphide bond formation is actually driven by electron transport. Disulphide isomerization requires that incorrect disulphides be attacked using a reduced catalyst, followed by the redonation of the disulphide, allowing alternative disulphide pairing. Two isomerases exist in Escherichia coli , DsbC and DsbG. The membrane protein DsbD maintains these disulphide isomerases in their reduced and thereby active form. DsbD is kept reduced by cytosolic thioredoxin in an NADPH-dependent reaction.en_US
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dc.format.mimetypeapplication/pdf
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dc.publisherBlackwell Science Ltden_US
dc.rights2002 Blackwell Science Ltd.en_US
dc.titleOxidative protein folding in bacteriaen_US
dc.typeArticleen_US
dc.subject.hlbsecondlevelMicrobiology and Immunologyen_US
dc.subject.hlbtoplevelScienceen_US
dc.description.peerreviewedPeer Revieweden_US
dc.contributor.affiliationotherGroupe de recherches metaboliques, Universite catholique de Louvain, UCL 75-39, B-1200 Brussels, Belgium.en_US
dc.identifier.pmid11967064en_US
dc.description.bitstreamurlhttp://deepblue.lib.umich.edu/bitstream/2027.42/75150/1/j.1365-2958.2002.02851.x.pdf
dc.identifier.doi10.1046/j.1365-2958.2002.02851.xen_US
dc.identifier.sourceMolecular Microbiologyen_US
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dc.owningcollnameInterdisciplinary and Peer-Reviewed


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