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dc.contributor.authorShouldice, Stephen R
dc.contributor.authorCho, Seung-Hyun
dc.contributor.authorBoyd, Dana
dc.contributor.authorHeras, Begona
dc.contributor.authorEser, Markus
dc.contributor.authorBeckwith, Jon
dc.contributor.authorRiggs, Paul
dc.contributor.authorMartin, Jennifer L
dc.contributor.authorBerkmen, Mehmet
dc.date.accessioned2017-09-01T03:56:46Z
dc.date.available2017-09-01T03:56:46Z
dc.date.issued2010
dc.identifier.issn0950-382X
dc.identifier.doi10.1111/j.1365-2958.2009.06952.x
dc.identifier.urihttp://hdl.handle.net/10072/345723
dc.description.abstractCurrent dogma dictates that bacterial proteins with misoxidized disulfide bonds are shuffled into correctly oxidized states by DsbC. There are two proposed mechanisms for DsbC activity. The first involves a DsbC-only model of substrate disulfide rearrangement. The second invokes cycles of reduction and oxidation of substrate disulfide bonds by DsbC and DsbA respectively. Here, we addressed whether the second mechanism is important in vivo by identifying whether a periplasmic reductase could complement DsbC. We screened for naturally occurring periplasmic reductases in Bacteroides fragilis, a bacterium chosen because we predicted it encodes reductases and has a reducing periplasm. We found that the B. fragilis periplasmic protein TrxP has a thioredoxin fold with an extended N-terminal region; that it is a very active reductase but a poor isomerase; and that it fully complements dsbC. These results provide direct in vivo evidence that correctly folded protein is achievable via cycles of oxidation and reduction.
dc.description.peerreviewedYes
dc.languageEnglish
dc.language.isoeng
dc.publisherBlackwell Publishing
dc.relation.ispartofpagefrom13
dc.relation.ispartofpageto28
dc.relation.ispartofissue1
dc.relation.ispartofjournalMolecular Microbiology
dc.relation.ispartofvolume75
dc.subject.fieldofresearchBiological sciences
dc.subject.fieldofresearchBiochemistry and cell biology not elsewhere classified
dc.subject.fieldofresearchAgricultural, veterinary and food sciences
dc.subject.fieldofresearchBiomedical and clinical sciences
dc.subject.fieldofresearchcode31
dc.subject.fieldofresearchcode310199
dc.subject.fieldofresearchcode30
dc.subject.fieldofresearchcode32
dc.titleIn vivo oxidative protein folding can be facilitated by oxidation-reduction cycling
dc.typeJournal article
dc.type.descriptionC1 - Articles
dc.type.codeC - Journal Articles
gro.hasfulltextNo Full Text
gro.griffith.authorMartin, Jennifer


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