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Volumn 44, Issue 7, 2012, Pages 623-627

Glutaredoxin serves as a reductant for methionine sulfoxide reductases with or without resolving cysteine

Author keywords

glutaredoxin; methionine sulfoxide reductase; reductant; thioredoxin

Indexed keywords

BACTERIAL PROTEIN; CYSTEINE; GLUTAREDOXIN; METHIONINE SULFOXIDE REDUCTASE; MSRB2 PROTEIN, HUMAN; REDUCING AGENT; TRANSCRIPTION FACTOR;

EID: 84863430482     PISSN: 16729145     EISSN: 17457270     Source Type: Journal    
DOI: 10.1093/abbs/gms038     Document Type: Article
Times cited : (27)

References (22)
  • 1
    • 35748932403 scopus 로고    scopus 로고
    • Methionine sulfoxide reductases: Selenoprotein forms and roles in antioxidant protein repair in mammals
    • Kim HY and Gladyshev VN. Methionine sulfoxide reductases: Selenoprotein forms and roles in antioxidant protein repair in mammals. Biochem J 2007, 407: 321-329.
    • (2007) Biochem J. , vol.407 , pp. 321-329
    • Kim, H.Y.1    Gladyshev, V.N.2
  • 2
    • 12844264123 scopus 로고    scopus 로고
    • Methionine sulfoxide reductases: History and cellular role in protecting against oxidative damage
    • Weissbach H, Resnick L and Brot N. Methionine sulfoxide reductases: History and cellular role in protecting against oxidative damage. Biochim Biophys Acta 2005, 1703: 203-212.
    • (2005) Biochim. Biophys. Acta , vol.1703 , pp. 203-212
    • Weissbach, H.1    Resnick, L.2    Brot, N.3
  • 3
    • 44549088533 scopus 로고    scopus 로고
    • The methionine sulfoxide reductases: Catalysis and substrate specificities
    • Boschi-Muller S, Gand A and Branlant G. The methionine sulfoxide reductases: Catalysis and substrate specificities. Arch Biochem Biophys 2008, 474: 266-273.
    • (2008) Arch. Biochem. Biophys. , vol.474 , pp. 266-273
    • Boschi-Muller, S.1    Gand, A.2    Branlant, G.3
  • 4
    • 0034612330 scopus 로고    scopus 로고
    • Thiol-disulfide exchange is involved in the catalytic mechanism of peptide methionine sulfoxide reductase
    • Lowther WT, Brot N, Weissbach H, Honek JF and Matthews BW. Thiol-disulfide exchange is involved in the catalytic mechanism of peptide methionine sulfoxide reductase. Proc Natl Acad Sci USA 2000, 97: 6463-6468.
    • (2000) Proc. Natl. Acad. Sci. USA , vol.97 , pp. 6463-6468
    • Lowther, W.T.1    Brot, N.2    Weissbach, H.3    Honek, J.F.4    Matthews, B.W.5
  • 5
    • 0034435463 scopus 로고    scopus 로고
    • Crystal structure of the Escherichia coli peptide methionine sulphoxide reductase at 1.9Å resolution
    • Tete-Favier F, Cobessi D, Boschi-Muller S, Azza S, Branlant G and Aubry A. Crystal structure of the Escherichia coli peptide methionine sulphoxide reductase at 1.9Å resolution. Structure 2000, 8: 1167-1178.
    • (2000) Structure , vol.8 , pp. 1167-1178
    • Tete-Favier, F.1    Cobessi, D.2    Boschi-Muller, S.3    Azza, S.4    Branlant, G.5    Aubry, A.6
  • 6
    • 0038154089 scopus 로고    scopus 로고
    • Structure of Mycobacterium tuberculosis methionine sulfoxide reductase A in complex with protein-bound methionine
    • Taylor AB, Benglis DM, Jr, Dhandayuthapani S and Hart PJ. Structure of Mycobacterium tuberculosis methionine sulfoxide reductase A in complex with protein-bound methionine. J Bacteriol 2003, 185: 4119-4126.
    • (2003) J. Bacteriol. , vol.185 , pp. 4119-4126
    • Taylor, A.B.1    Benglis Jr., D.M.2    Dhandayuthapani, S.3    Hart, P.J.4
  • 7
    • 65349106531 scopus 로고    scopus 로고
    • Structural and kinetic analysis of an MsrA-MsrB fusion protein from Streptococcus pneumoniae
    • Kim YK, Shin YJ, Lee WH, Kim HY and Hwang KY. Structural and kinetic analysis of an MsrA-MsrB fusion protein from Streptococcus pneumoniae. Mol Microbiol 2009, 72: 699-709.
    • (2009) Mol. Microbiol. , vol.72 , pp. 699-709
    • Kim, Y.K.1    Shin, Y.J.2    Lee, W.H.3    Kim, H.Y.4    Hwang, K.Y.5
  • 8
    • 65249142849 scopus 로고    scopus 로고
    • Protein-repairing methionine sulfoxide reductases in photosynthetic organisms: Gene organization, reduction mechanisms, and physiological roles
    • Tarrago L, Laugier E and Rey P. Protein-repairing methionine sulfoxide reductases in photosynthetic organisms: Gene organization, reduction mechanisms, and physiological roles. Mol Plant 2009, 2: 202-217.
    • (2009) Mol. Plant. , vol.2 , pp. 202-217
    • Tarrago, L.1    Laugier, E.2    Rey, P.3
  • 9
    • 61449267536 scopus 로고    scopus 로고
    • The selenoproteome of Clostridium sp OhILAs: Characterization of anaerobic bacterial selenoprotein methionine sulfoxide reductase A
    • Kim HY, Zhang Y, Lee BC, Kim JR and Gladyshev VN. The selenoproteome of Clostridium sp. OhILAs: Characterization of anaerobic bacterial selenoprotein methionine sulfoxide reductase A. Proteins 2009, 74: 1008-1017.
    • (2009) Proteins , vol.74 , pp. 1008-1017
    • Kim, H.Y.1    Zhang, Y.2    Lee, B.C.3    Kim, J.R.4    Gladyshev, V.N.5
  • 10
    • 33751220854 scopus 로고    scopus 로고
    • Catalytic advantages provided by selenocysteine in methionine-S-sulfoxide reductases
    • Kim HY, Fomenko DE, Yoon YE and Gladyshev VN. Catalytic advantages provided by selenocysteine in methionine-S-sulfoxide reductases. Biochemistry 2006, 45: 13697-13704.
    • (2006) Biochemistry , vol.45 , pp. 13697-13704
    • Kim, H.Y.1    Fomenko, D.E.2    Yoon, Y.E.3    Gladyshev, V.N.4
  • 11
    • 0037020249 scopus 로고    scopus 로고
    • Reaction mechanism, evolutionary analysis, and role of zinc in Drosophila methionine- R-sulfoxide reductase
    • Kumar RA, Koc A, Cerny RL and Gladyshev VN. Reaction mechanism, evolutionary analysis, and role of zinc in Drosophila methionine- R-sulfoxide reductase. J Biol Chem 2002, 277: 37527-37535.
    • (2002) J. Biol. Chem. , vol.277 , pp. 37527-37535
    • Kumar, R.A.1    Koc, A.2    Cerny, R.L.3    Gladyshev, V.N.4
  • 12
    • 33845428642 scopus 로고    scopus 로고
    • Thioredoxin and related molecules-from biology to health and disease
    • Lillig CH and Holmgren A. Thioredoxin and related molecules-from biology to health and disease. Antioxid Redox Signal 2007, 9: 25-47.
    • (2007) Antioxid Redox Signal , vol.9 , pp. 25-47
    • Lillig, C.H.1    Holmgren, A.2
  • 13
    • 77952311188 scopus 로고    scopus 로고
    • Thioredoxin and thioredoxin reductase: Current research with special reference to human disease
    • Holmgren A and Lu J. Thioredoxin and thioredoxin reductase: Current research with special reference to human disease. Biochem Biophys Res Commun 2010, 396: 120-124.
    • (2010) Biochem. Biophys. Res. Commun. , vol.396 , pp. 120-124
    • Holmgren, A.1    Lu, J.2
  • 14
    • 43549109795 scopus 로고    scopus 로고
    • Thioredoxin as a reducing agent for mammalian methionine sulfoxide reductases B lacking resolving cysteine
    • Kim HY and Kim JR. Thioredoxin as a reducing agent for mammalian methionine sulfoxide reductases B lacking resolving cysteine. Biochem Biophys Res Commun 2008, 371: 490-494.
    • (2008) Biochem. Biophys. Res. Commun. , vol.371 , pp. 490-494
    • Kim, H.Y.1    Kim, J.R.2
  • 15
    • 52049084778 scopus 로고    scopus 로고
    • An anaerobic bacterial MsrB model reveals catalytic mechanisms, advantages, and disadvantages provided by selenocysteine and cysteine in reduction of methionine-R-sulfoxide
    • Lee TH and Kim HY. An anaerobic bacterial MsrB model reveals catalytic mechanisms, advantages, and disadvantages provided by selenocysteine and cysteine in reduction of methionine-R-sulfoxide. Arch Biochem Biophys 2008, 478: 175-180.
    • (2008) Arch. Biochem. Biophys. , vol.478 , pp. 175-180
    • Lee, T.H.1    Kim, H.Y.2
  • 16
    • 34548503203 scopus 로고    scopus 로고
    • Specificity of thioredoxins and glutaredoxins as electron donors to two distinct classes of Arabidopsis plastidial methionine sulfoxide reductases B
    • Vieira Dos Santos C, Laugier E, Tarrago L, Massot V, Issakidis-Bourguet E, Rouhier N and Rey P. Specificity of thioredoxins and glutaredoxins as electron donors to two distinct classes of Arabidopsis plastidial methionine sulfoxide reductases B. FEBS Lett 2007, 581: 4371-4376.
    • (2007) FEBS Lett. , vol.581 , pp. 4371-4376
    • Vieira Dos Santos, C.1    Laugier, E.2    Tarrago, L.3    Massot, V.4    Issakidis-Bourguet, E.5    Rouhier, N.6    Rey, P.7
  • 18
    • 28844480498 scopus 로고    scopus 로고
    • Hudemann C and Lillig Thiol redox control via thioredoxin and glutaredoxin systems
    • Holmgren A, Johansson C, Berndt C, Lonn ME, Hudemann C and Lillig CH. Thiol redox control via thioredoxin and glutaredoxin systems. Biochem Soc Trans 2005, 33: 1375-1377.
    • (2005) Biochem. Soc. Trans. , vol.33 , pp. 1375-1377
    • Holmgren, A.1    Johansson, C.2    Berndt, C.3    Lonn, M.E.4
  • 19
    • 67650511700 scopus 로고    scopus 로고
    • Regeneration mechanisms of Arabidopsis thaliana methionine sulfoxide reductases B by glutaredoxins and thioredoxins
    • Tarrago L, Laugier E, Zaffagnini M, Marchand C, Le Marechal P, Rouhier N and Lemaire SD, et al. Regeneration mechanisms of Arabidopsis thaliana methionine sulfoxide reductases B by glutaredoxins and thioredoxins. J Biol Chem 2009, 284: 18963-18971.
    • (2009) J. Biol. Chem. , vol.284 , pp. 18963-18971
    • Tarrago, L.1    Laugier, E.2    Zaffagnini, M.3    Marchand, C.4    Le Marechal, P.5    Rouhier, N.6    Lemaire, S.D.7
  • 20
    • 79951808111 scopus 로고    scopus 로고
    • Tandem use of selenocysteine: Adaptation of a selenoprotein glutaredoxin for reduction of selenoprotein methionine sulfoxide reductase
    • Kim MJ, Lee BC, Jeong J, Lee KJ, Hwang KY, Gladyshev VN and Kim HY. Tandem use of selenocysteine: Adaptation of a selenoprotein glutaredoxin for reduction of selenoprotein methionine sulfoxide reductase. Mol Microbiol 2011, 79: 1194-1203.
    • (2011) Mol. Microbiol. , vol.79 , pp. 1194-1203
    • Kim, M.J.1    Lee, B.C.2    Jeong, J.3    Lee, K.J.4    Hwang, K.Y.5    Gladyshev, V.N.6    Kim, H.Y.7
  • 21
    • 20144375447 scopus 로고    scopus 로고
    • Role of structural and functional elements of mouse methionine-S- sulfoxide reductase in its subcellular distribution
    • Kim HY and Gladyshev VN. Role of structural and functional elements of mouse methionine-S-sulfoxide reductase in its subcellular distribution. Biochemistry 2005, 44: 8059-8067.
    • (2005) Biochemistry , vol.44 , pp. 8059-8067
    • Kim, H.Y.1    Gladyshev, V.N.2
  • 22
    • 33747369873 scopus 로고    scopus 로고
    • Characterization of alternative cytosolic forms and cellular targets of mouse mitochondrial thioredoxin reductase
    • Turanov AA, Su D and Gladyshev VN. Characterization of alternative cytosolic forms and cellular targets of mouse mitochondrial thioredoxin reductase. J Biol Chem 2006, 281: 22953-22963.
    • (2006) J. Biol. Chem. , vol.281 , pp. 22953-22963
    • Turanov, A.A.1    Su, D.2    Gladyshev, V.N.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.