2007
DOI: 10.1074/jbc.m705291200
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The CXXC Motif Is More than a Redox Rheostat

Abstract: The CXXC active-site motif of thiol-disulfide oxidoreductases is thought to act as a redox rheostat, the sequence of which determines its reduction potential and functional properties. We tested this idea by selecting for mutants of the CXXC motif in a reducing oxidoreductase (thioredoxin) that complement null mutants of a very oxidizing oxidoreductase, DsbA. We found that altering the CXXC motif affected not only the reduction potential of the protein, but also its ability to function as a disulfide isomerase… Show more

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Cited by 127 publications
(134 citation statements)
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“…An important role for the proline at the second position of the CXXC motif has been demonstrated for DsbA, the major oxidizing Trx-like protein in E. coli, and a CPXC motif is a factor contributing to the oxidizing power of thioredoxin that is targeted to the periplasmic space of bacteria (30,31). Its presence in VKOR-interacting redox partners is consistent with a role in oxidative protein folding.…”
Section: Discussionmentioning
confidence: 68%
“…An important role for the proline at the second position of the CXXC motif has been demonstrated for DsbA, the major oxidizing Trx-like protein in E. coli, and a CPXC motif is a factor contributing to the oxidizing power of thioredoxin that is targeted to the periplasmic space of bacteria (30,31). Its presence in VKOR-interacting redox partners is consistent with a role in oxidative protein folding.…”
Section: Discussionmentioning
confidence: 68%
“…There is a remarkable correlation between the standard redox potential of these enzymes and their physiological role; indeed the members with the lowest redox potentials catalyze reducing processes in vivo (Trx, Ϫ270 mV (4); and glutaredoxin, Ϫ233 to Ϫ198 mV (5)), whereas the protein folding catalysts are strong oxidizing agents (PDI, Ϫ175 to Ϫ147 mV (6, 7); and DsbA, Ϫ163 to Ϫ80 mV (8)). Exceptions are the thioredoxin-like proteins anchored to the inner bacterial membrane.…”
mentioning
confidence: 99%
“…Generally, this results in an oxidoreductase with redox properties similar to that of the oxidoreductase from where the dipeptide originated (18,(21)(22)(23). To this end, in two state-of-the-art papers, the Glockshuber group changed the XX dipeptide of the prototype reductase Trx (CGPC) and oxidase DsbA (CPHC) into the protein-disulfide isomerase type (CGHC), the glutaredoxin (Grx) type (CPYC), and the DsbA or Trx type, respectively (22,23).…”
Section: Sno (mentioning
confidence: 99%
“…The plasmids used for the expression of wild type E. coli DsbC, DsbG, YbiS, and Trx-1 have been described previously (9,10,21). The P110GY111P (CGPC) and T200M mutations were inserted in DsbG using the Stratagene QuikChange mutagenesis kit, using the CGPC-fw (3Ј-gcc gat ccg ttc tgc gga cct tgt aaa cag ttc tgg-5Ј) and CGPC-rv (3Ј-cca gaa ctg ttt aça agg tcc gca gaa cgg atc ggc-5Ј) primers for the CGPC mutant and the T200M-fw (3Ј-gca aat gtc atg ccg gct atc-5Ј) and T200M-rv (3Ј-gat agc cgg cat gac att tgc-5Ј) primers for the T200M mutant.…”
Section: Plasmids and Site-directed Mutagenesismentioning
confidence: 99%
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