메뉴 건너뛰기




Volumn 55, Issue , 2001, Pages 21-48

Roles of thiol-redox pathways in bacteria

Author keywords

Disulfide bond; Escherichia coli; Glutaredoxin; Oxidative stress; Thioredoxin

Indexed keywords

GLUTATHIONE; GLUTATHIONE REDUCTASE; THIOL DERIVATIVE; THIOREDOXIN; THIOREDOXIN REDUCTASE;

EID: 0034770083     PISSN: 00664227     EISSN: None     Source Type: Book Series    
DOI: 10.1146/annurev.micro.55.1.21     Document Type: Review
Times cited : (291)

References (142)
  • 3
    • 0030695902 scopus 로고    scopus 로고
    • Redox potentials of glutaredoxins and other thiol-disulfide oxidoreductases of the thioredoxin superfamily determined by direct protein-protein redox equilibria
    • (1997) J. Biol. Chem. , vol.272 , pp. 30780-30786
    • Åslund, F.1    Berndt, K.D.2    Holmgren, A.3
  • 16
    • 0025923587 scopus 로고
    • 2 assimilation in oxygenic photosynthesis: The ferredoxin/thioredoxin system. Perspective on its discovery, present status, and future development
    • (1991) Arch. Biochem. Biophys. , vol.288 , pp. 1-9
    • Buchanan, B.B.1
  • 19
    • 0033767925 scopus 로고    scopus 로고
    • Roles of the glutathione- and thioredoxin-dependent reduction systems in the Escherichia coli and Saccharomyces cerevisiae responses to oxidative stress
    • (2000) Annu. Rev. Microbiol. , vol.54 , pp. 439-461
    • Carmel-Harel, O.1    Storz, G.2
  • 21
    • 0034011364 scopus 로고    scopus 로고
    • Transfer of electrons across the cytoplasmic membrane by DsbD, a membrane protein involved in thiol-disulphide exchange and protein folding in the bacterial periplasm
    • (2000) Mol. Microbiol. , vol.35 , pp. 1099-1109
    • Chung, J.1    Chen, T.2    Missiakas, D.3
  • 22
    • 0028930524 scopus 로고
    • The biogenesis of c-type cytochromes in Escherichia coli requires a membrane-bound protein, DipZ, with a protein disulphide isomerase-like domain
    • (1995) Mol. Microbiol. , vol.15 , pp. 1139-1150
    • Crooke, H.1    Cole, J.2
  • 35
    • 0032475938 scopus 로고    scopus 로고
    • Functional analysis of the Escherichia coli genome using the sequence-to-structure-to-function paradigm: Identification of proteins exhibiting the glutaredoxin/thioredoxin disulfide oxidoreductase activity
    • (1998) J. Mol. Biol. , vol.282 , pp. 703-711
    • Fetrow, J.S.1    Godzik, A.2    Skolnick, J.3
  • 37
    • 0033213605 scopus 로고    scopus 로고
    • Ero1p oxidizes protein disulfide isomerase in a pathway for disulfide bond formation in the endoplasmic reticulum
    • (1999) Mol. Cell. , vol.4 , pp. 469-477
    • Frand, A.R.1    Kaiser, C.A.2
  • 38
    • 0034494605 scopus 로고    scopus 로고
    • Two pairs of conserved cysteines are required for the oxidative activity of Ero1p in protein disulfide bond formation in the endoplasmic reticulum
    • (2000) Mol. Biol. Cell. , vol.11 , pp. 2833-2843
    • Frand, A.R.1    Kaiser, C.A.2
  • 52
    • 0030787850 scopus 로고    scopus 로고
    • In vitro and in vivo redox states of the Escherichia coli periplasmic oxidoreductases DsbA and DsbC
    • (1997) Biochemistry , vol.36 , pp. 10067-10072
    • Joly, J.C.1    Swartz, J.R.2
  • 60
    • 0034703766 scopus 로고    scopus 로고
    • Transmembrane electron transfer by the membrane protein DsbD occurs via a disulfide bond cascade
    • (2000) Cell , vol.103 , pp. 769-779
    • Katzen, F.1    Beckwith, J.2
  • 62
    • 0033106153 scopus 로고    scopus 로고
    • Respiratory chain strongly oxidizes the CXXC motif of DsbB in the Escherichia coli disulfide bond formation pathway
    • (1999) EMBO J. , vol.18 , pp. 1192-1198
    • Kobayashi, T.1    Ito, K.2
  • 68
    • 0028057226 scopus 로고
    • YAP1 dependent activation of TRX2 is essential for the response of Saccharomyces cerevisiae to oxidative stress by hydroperoxides
    • (1994) EMBO J. , vol.13 , pp. 655-664
    • Kuge, S.1    Jones, N.2
  • 69
    • 0001356912 scopus 로고    scopus 로고
    • A thioredoxin from the hyperthermophilic archaeon Methanococcus jannaschii has a glutaredoxin-like fold but thioredoxin-like activities
    • (2000) Biochemistry , vol.39 , pp. 6652-6659
    • Lee, D.Y.1    Ahn, B.Y.2    Kim, K.S.3
  • 75
    • 0028021929 scopus 로고
    • Expression, purification and functional properties of a soluble form of Bradyrhizobium japonicum TlpA, a thioredoxin-like protein
    • (1994) Eur. J. Biochem. , vol.223 , pp. 339-344
    • Loferer, H.1    Hennecke, H.2
  • 96
    • 0032190375 scopus 로고    scopus 로고
    • sigmaR, an RNA polymerase sigma factor that modulates expression of the thioredoxin system in response to oxidative stress in Streptomyces coelicolor A3(2)
    • (1998) EMBO J. , vol.17 , pp. 5776-5782
    • Paget, M.S.1    Kang, J.G.2    Roe, J.H.3    Buttner, M.J.4
  • 100
    • 0034612366 scopus 로고    scopus 로고
    • AhpF can be dissected into two functional units: Tandem repeats of two thioredoxin-like folds in the N-terminus mediate electron transfer from the thioredoxin reductase-like C terminus to AhpC
    • (2000) Biochemistry , vol.39 , pp. 6602-6615
    • Poole, L.B.1    Godzik, A.2    Nayeem, A.3    Schmitt, J.D.4
  • 104
    • 0034254337 scopus 로고    scopus 로고
    • Attachment of the N-terminal domain of Salmonella typhimurium AhpF to Escherichia coli thioredoxin reductase confers AhpC reductase activity but does not affect thioredoxin reductase activity
    • (2000) Biochemistry , vol.39 , pp. 8859-8869
    • Reynolds, C.M.1    Poole, L.B.2
  • 122
    • 0033230589 scopus 로고    scopus 로고
    • Six conserved cysteines of the membrane protein DsbD are required for the transfer of electrons from the cytoplasm to the periplasm of Escherichia coli
    • (1999) EMBO J. , vol.18 , pp. 5963-5971
    • Stewart, E.J.1    Katzen, F.2    Beckwith, J.3
  • 123
    • 0034725691 scopus 로고    scopus 로고
    • The N-terminal sequence (residues 1-65) is essential for dimerization, activities, and peptide binding of Escherichia coli DsbC
    • (2000) J. Biol. Chem. , vol.275 , pp. 22743-22749
    • Sun, X.X.1    Wang, C.C.2
  • 126
    • 0019795159 scopus 로고
    • Assimilatory sulfate reduction in Escherichia coli: Identification of the alternate cofactor for adenosine 3′-phosphate 5′-phosphosulfate reductase as glutaredoxin
    • (1981) J. Bacteriol. , vol.146 , pp. 1059-1066
    • Tsang, M.L.1
  • 128
  • 135
    • 0028785378 scopus 로고
    • Mechanism and structure of thioredoxin reductase from Escherichia coli
    • (1995) FASEB J. , vol.9 , pp. 1267-1276
    • Williams C.H., Jr.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.