메뉴 건너뛰기




Volumn 1794, Issue 4, 2009, Pages 716-721

Structural and mechanistic analyses of yeast mitochondrial thioredoxin Trx3 reveal putative function of its additional cysteine residues

Author keywords

Crystal structure; Mitochondrion; S nitrosylation; Saccharomyces cerevisiae; Thioredoxin

Indexed keywords

CARRIER PROTEINS AND BINDING PROTEINS; CYSTEINE; THIOREDOXIN 1; THIOREDOXIN 3; UNCLASSIFIED DRUG;

EID: 61649116904     PISSN: 15709639     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbapap.2008.12.016     Document Type: Article
Times cited : (17)

References (46)
  • 1
    • 78651146370 scopus 로고
    • Enzymatic synthesis of deoxyribonucleotides. Iv. Isolation and characterization of thioredoxin, the hydrogen donor from Escherichia coli B
    • Laurent T.C., Moore E.C., and Reichard P. Enzymatic synthesis of deoxyribonucleotides. Iv. Isolation and characterization of thioredoxin, the hydrogen donor from Escherichia coli B. J. Biol. Chem. 239 (1964) 3436-3444
    • (1964) J. Biol. Chem. , vol.239 , pp. 3436-3444
    • Laurent, T.C.1    Moore, E.C.2    Reichard, P.3
  • 2
    • 0028344541 scopus 로고
    • Distinct effects of thioredoxin and antioxidants on the activation of transcription factors NF-kappa B and AP-1
    • Schenk H., Klein M., Erdbrugger W., Droge W., and Schulze-Osthoff K. Distinct effects of thioredoxin and antioxidants on the activation of transcription factors NF-kappa B and AP-1. Proc. Natl. Acad. Sci. U. S. A. 91 (1994) 1672-1676
    • (1994) Proc. Natl. Acad. Sci. U. S. A. , vol.91 , pp. 1672-1676
    • Schenk, H.1    Klein, M.2    Erdbrugger, W.3    Droge, W.4    Schulze-Osthoff, K.5
  • 3
    • 0023035960 scopus 로고
    • The role of thioredoxin in filamentous phage assembly. Construction, isolation, and characterization of mutant thioredoxins
    • Russel M., and Model P. The role of thioredoxin in filamentous phage assembly. Construction, isolation, and characterization of mutant thioredoxins. J. Biol. Chem. 261 (1986) 14997-15005
    • (1986) J. Biol. Chem. , vol.261 , pp. 14997-15005
    • Russel, M.1    Model, P.2
  • 4
    • 34047204205 scopus 로고    scopus 로고
    • 3'-Phosphoadenosine-5'-phosphosulfate reductase in complex with thioredoxin: a structural snapshot in the catalytic cycle
    • Chartron J., Shiau C., Stout C.D., and Carroll K.S. 3'-Phosphoadenosine-5'-phosphosulfate reductase in complex with thioredoxin: a structural snapshot in the catalytic cycle. Biochemistry 46 (2007) 3942-3951
    • (2007) Biochemistry , vol.46 , pp. 3942-3951
    • Chartron, J.1    Shiau, C.2    Stout, C.D.3    Carroll, K.S.4
  • 5
    • 0142182386 scopus 로고    scopus 로고
    • The role of thioredoxin in the aging process: involvement of oxidative stress
    • Yoshida T., Oka S., Masutani H., Nakamura H., and Yodoi J. The role of thioredoxin in the aging process: involvement of oxidative stress. Antioxid. Redox. Signal. 5 (2003) 563-570
    • (2003) Antioxid. Redox. Signal. , vol.5 , pp. 563-570
    • Yoshida, T.1    Oka, S.2    Masutani, H.3    Nakamura, H.4    Yodoi, J.5
  • 8
    • 0036798856 scopus 로고    scopus 로고
    • Redox regulatory and anti-apoptotic functions of thioredoxin depend on S-nitrosylation at cysteine 69
    • Haendeler J., Hoffmann J., Tischler V., Berk B.C., Zeiher A.M., and Dimmeler S. Redox regulatory and anti-apoptotic functions of thioredoxin depend on S-nitrosylation at cysteine 69. Nat. Cell. Biol. 4 (2002) 743-749
    • (2002) Nat. Cell. Biol. , vol.4 , pp. 743-749
    • Haendeler, J.1    Hoffmann, J.2    Tischler, V.3    Berk, B.C.4    Zeiher, A.M.5    Dimmeler, S.6
  • 9
    • 52049087608 scopus 로고    scopus 로고
    • Regulation of the catalytic activity and structure of human thioredoxin 1 via oxidation and S-nitrosylation of cysteine residues
    • Hashemy S.I., and Holmgren A. Regulation of the catalytic activity and structure of human thioredoxin 1 via oxidation and S-nitrosylation of cysteine residues. J. Biol. Chem. 283 (2008) 21890-21898
    • (2008) J. Biol. Chem. , vol.283 , pp. 21890-21898
    • Hashemy, S.I.1    Holmgren, A.2
  • 10
    • 33846783114 scopus 로고    scopus 로고
    • Buried S-nitrosocysteine revealed in crystal structures of human thioredoxin
    • Weichsel A., Brailey J.L., and Montfort W.R. Buried S-nitrosocysteine revealed in crystal structures of human thioredoxin. Biochemistry 46 (2007) 1219-1227
    • (2007) Biochemistry , vol.46 , pp. 1219-1227
    • Weichsel, A.1    Brailey, J.L.2    Montfort, W.R.3
  • 12
    • 33645560710 scopus 로고    scopus 로고
    • Mitochondrial cytochrome oxidase produces nitric oxide under hypoxic conditions: implications for oxygen sensing and hypoxic signaling in eukaryotes
    • Castello P.R., David P.S., McClure T., Crook Z., and Poyton R.O. Mitochondrial cytochrome oxidase produces nitric oxide under hypoxic conditions: implications for oxygen sensing and hypoxic signaling in eukaryotes. Cell. Metab. 3 (2006) 277-287
    • (2006) Cell. Metab. , vol.3 , pp. 277-287
    • Castello, P.R.1    David, P.S.2    McClure, T.3    Crook, Z.4    Poyton, R.O.5
  • 13
    • 14844316642 scopus 로고    scopus 로고
    • Yeast flavohemoglobin, a nitric oxide oxidoreductase, is located in both the cytosol and the mitochondrial matrix: effects of respiration, anoxia, and the mitochondrial genome on its intracellular level and distribution
    • Cassanova N., O'Brien K.M., Stahl B.T., McClure T., and Poyton R.O. Yeast flavohemoglobin, a nitric oxide oxidoreductase, is located in both the cytosol and the mitochondrial matrix: effects of respiration, anoxia, and the mitochondrial genome on its intracellular level and distribution. J. Biol. Chem. 280 (2005) 7645-7653
    • (2005) J. Biol. Chem. , vol.280 , pp. 7645-7653
    • Cassanova, N.1    O'Brien, K.M.2    Stahl, B.T.3    McClure, T.4    Poyton, R.O.5
  • 16
    • 0037085384 scopus 로고    scopus 로고
    • Cooperation of yeast peroxiredoxins Tsa1p and Tsa2p in the cellular defense against oxidative and nitrosative stress
    • Wong C.M., Zhou Y., Ng R.W., Kung Hf H.F., and Jin D.Y. Cooperation of yeast peroxiredoxins Tsa1p and Tsa2p in the cellular defense against oxidative and nitrosative stress. J. Biol. Chem. 277 (2002) 5385-5394
    • (2002) J. Biol. Chem. , vol.277 , pp. 5385-5394
    • Wong, C.M.1    Zhou, Y.2    Ng, R.W.3    Kung Hf, H.F.4    Jin, D.Y.5
  • 17
    • 0035932413 scopus 로고    scopus 로고
    • A metabolic enzyme for S-nitrosothiol conserved from bacteria to humans
    • Liu L., Hausladen A., Zeng M., Que L., Heitman J., and Stamler J.S. A metabolic enzyme for S-nitrosothiol conserved from bacteria to humans. Nature 410 (2001) 490-494
    • (2001) Nature , vol.410 , pp. 490-494
    • Liu, L.1    Hausladen, A.2    Zeng, M.3    Que, L.4    Heitman, J.5    Stamler, J.S.6
  • 18
    • 0033525509 scopus 로고    scopus 로고
    • Identification and functional characterization of a novel mitochondrial thioredoxin system in Saccharomyces cerevisiae
    • Pedrajas J.R., Kosmidou E., Miranda-Vizuete A., Gustafsson J.A., Wright A.P., and Spyrou G. Identification and functional characterization of a novel mitochondrial thioredoxin system in Saccharomyces cerevisiae. J. Biol. Chem. 274 (1999) 6366-6373
    • (1999) J. Biol. Chem. , vol.274 , pp. 6366-6373
    • Pedrajas, J.R.1    Kosmidou, E.2    Miranda-Vizuete, A.3    Gustafsson, J.A.4    Wright, A.P.5    Spyrou, G.6
  • 19
    • 33750597744 scopus 로고    scopus 로고
    • Expression, purification, crystallization and preliminary X-ray diffraction analysis of mitochondrial thioredoxin Trx3 from Saccharomyces cerevisiae
    • Bao R., Chen Y.X., Zhang Y., and Zhou C.Z. Expression, purification, crystallization and preliminary X-ray diffraction analysis of mitochondrial thioredoxin Trx3 from Saccharomyces cerevisiae. Acta Crystallograph. Sect. F. Struct. Biol. Cryst. Commun. 62 (2006) 1161-1163
    • (2006) Acta Crystallograph. Sect. F. Struct. Biol. Cryst. Commun. , vol.62 , pp. 1161-1163
    • Bao, R.1    Chen, Y.X.2    Zhang, Y.3    Zhou, C.Z.4
  • 20
    • 2642699794 scopus 로고
    • Rapid and efficient site-specific mutagenesis without phenotypic selection
    • Kunkel T.A. Rapid and efficient site-specific mutagenesis without phenotypic selection. Proc. Natl. Acad. Sci. U. S. A. 82 (1985) 488-492
    • (1985) Proc. Natl. Acad. Sci. U. S. A. , vol.82 , pp. 488-492
    • Kunkel, T.A.1
  • 21
    • 0033212815 scopus 로고    scopus 로고
    • Integration of macromolecular diffraction data
    • Leslie A.G. Integration of macromolecular diffraction data. Acta Crystallogr. D. Biol. Crystallogr. 55 (1999) 1696-1702
    • (1999) Acta Crystallogr. D. Biol. Crystallogr. , vol.55 , pp. 1696-1702
    • Leslie, A.G.1
  • 22
    • 0028103275 scopus 로고
    • The CCP4 suite: programs for protein crystallography
    • Project C.C. The CCP4 suite: programs for protein crystallography. Acta. Crystallogr. D. Biol. Crystallogr. 50 (1994) 760-763
    • (1994) Acta. Crystallogr. D. Biol. Crystallogr. , vol.50 , pp. 760-763
    • Project, C.C.1
  • 24
    • 84889120137 scopus 로고
    • Improved methods for building protein models in electron density maps and the location of errors in these models
    • Jones T.A., Zou J.Y., Cowan S.W., and Kjeldgaard M. Improved methods for building protein models in electron density maps and the location of errors in these models. Acta Crystallogr. A. 47 Pt 2 (1991) 110-119
    • (1991) Acta Crystallogr. A. , vol.47 , Issue.PART 2 , pp. 110-119
    • Jones, T.A.1    Zou, J.Y.2    Cowan, S.W.3    Kjeldgaard, M.4
  • 28
    • 0018728098 scopus 로고
    • Reduction of disulfides by thioredoxin. Exceptional reactivity of insulin and suggested functions of thioredoxin in mechanism of hormone action
    • Holmgren A. Reduction of disulfides by thioredoxin. Exceptional reactivity of insulin and suggested functions of thioredoxin in mechanism of hormone action. J. Biol. Chem. 254 (1979) 9113-9119
    • (1979) J. Biol. Chem. , vol.254 , pp. 9113-9119
    • Holmgren, A.1
  • 29
    • 33845648451 scopus 로고    scopus 로고
    • Crystal structure of the yeast cytoplasmic thioredoxin Trx2
    • Bao R., Chen Y., Tang Y.J., Janin J., and Zhou C.Z. Crystal structure of the yeast cytoplasmic thioredoxin Trx2. Proteins 66 (2007) 246-249
    • (2007) Proteins , vol.66 , pp. 246-249
    • Bao, R.1    Chen, Y.2    Tang, Y.J.3    Janin, J.4    Zhou, C.Z.5
  • 30
    • 0030585429 scopus 로고    scopus 로고
    • Crystal structures of reduced, oxidized, and mutated human thioredoxins: evidence for a regulatory homodimer
    • Weichsel A., Gasdaska J.R., Powis G., and Montfort W.R. Crystal structures of reduced, oxidized, and mutated human thioredoxins: evidence for a regulatory homodimer. Structure 4 (1996) 735-751
    • (1996) Structure , vol.4 , pp. 735-751
    • Weichsel, A.1    Gasdaska, J.R.2    Powis, G.3    Montfort, W.R.4
  • 31
    • 11844280984 scopus 로고    scopus 로고
    • Comparative structural analysis of oxidized and reduced thioredoxin from Drosophila melanogaster
    • Wahl M.C., Irmler A., Hecker B., Schirmer R.H., and Becker K. Comparative structural analysis of oxidized and reduced thioredoxin from Drosophila melanogaster. J. Mol. Biol. 345 (2005) 1119-1130
    • (2005) J. Mol. Biol. , vol.345 , pp. 1119-1130
    • Wahl, M.C.1    Irmler, A.2    Hecker, B.3    Schirmer, R.H.4    Becker, K.5
  • 33
    • 25844464168 scopus 로고    scopus 로고
    • Crystal structures of oxidized and reduced forms of human mitochondrial thioredoxin 2
    • Smeets A., Evrard C., Landtmeters M., Marchand C., Knoops B., and Declercq J.P. Crystal structures of oxidized and reduced forms of human mitochondrial thioredoxin 2. Protein Sci. 14 (2005) 2610-2621
    • (2005) Protein Sci. , vol.14 , pp. 2610-2621
    • Smeets, A.1    Evrard, C.2    Landtmeters, M.3    Marchand, C.4    Knoops, B.5    Declercq, J.P.6
  • 35
    • 0029645581 scopus 로고
    • Crystal structure of thioredoxin-2 from Anabaena
    • Saarinen M., Gleason F.K., and Eklund H. Crystal structure of thioredoxin-2 from Anabaena. Structure 3 (1995) 1097-1108
    • (1995) Structure , vol.3 , pp. 1097-1108
    • Saarinen, M.1    Gleason, F.K.2    Eklund, H.3
  • 36
    • 0028886558 scopus 로고
    • Ionisation of cysteine residues at the termini of model alpha-helical peptides. Relevance to unusual thiol pKa values in proteins of the thioredoxin family
    • Kortemme T., and Creighton T.E. Ionisation of cysteine residues at the termini of model alpha-helical peptides. Relevance to unusual thiol pKa values in proteins of the thioredoxin family. J. Mol. Biol. 253 (1995) 799-812
    • (1995) J. Mol. Biol. , vol.253 , pp. 799-812
    • Kortemme, T.1    Creighton, T.E.2
  • 37
    • 0041856170 scopus 로고    scopus 로고
    • Redox potential of human thioredoxin 1 and identification of a second dithiol/disulfide motif
    • Watson W.H., Pohl J., Montfort W.R., Stuchlik O., Reed M.S., Powis G., and Jones D.P. Redox potential of human thioredoxin 1 and identification of a second dithiol/disulfide motif. J. Biol. Chem. 278 (2003) 33408-33415
    • (2003) J. Biol. Chem. , vol.278 , pp. 33408-33415
    • Watson, W.H.1    Pohl, J.2    Montfort, W.R.3    Stuchlik, O.4    Reed, M.S.5    Powis, G.6    Jones, D.P.7
  • 38
    • 0030671351 scopus 로고    scopus 로고
    • Human thioredoxin homodimers: regulation by pH, role of aspartate 60, and crystal structure of the aspartate 60 -> asparagine mutant
    • Andersen J.F., Sanders D.A., Gasdaska J.R., Weichsel A., Powis G., and Montfort W.R. Human thioredoxin homodimers: regulation by pH, role of aspartate 60, and crystal structure of the aspartate 60 -> asparagine mutant. Biochemistry 36 (1997) 13979-13988
    • (1997) Biochemistry , vol.36 , pp. 13979-13988
    • Andersen, J.F.1    Sanders, D.A.2    Gasdaska, J.R.3    Weichsel, A.4    Powis, G.5    Montfort, W.R.6
  • 39
    • 0030956929 scopus 로고    scopus 로고
    • (S)NO signals: translocation, regulation, and a consensus motif
    • Stamler J.S., Toone E.J., Lipton S.A., and Sucher N.J. (S)NO signals: translocation, regulation, and a consensus motif. Neuron 18 (1997) 691-696
    • (1997) Neuron , vol.18 , pp. 691-696
    • Stamler, J.S.1    Toone, E.J.2    Lipton, S.A.3    Sucher, N.J.4
  • 41
    • 34547427294 scopus 로고    scopus 로고
    • Thioredoxin is required for S-nitrosation of procaspase-3 and the inhibition of apoptosis in Jurkat cells
    • Mitchell D.A., Morton S.U., Fernhoff N.B., and Marletta M.A. Thioredoxin is required for S-nitrosation of procaspase-3 and the inhibition of apoptosis in Jurkat cells. Proc. Natl. Acad. Sci. U. S. A. 104 (2007) 11609-11614
    • (2007) Proc. Natl. Acad. Sci. U. S. A. , vol.104 , pp. 11609-11614
    • Mitchell, D.A.1    Morton, S.U.2    Fernhoff, N.B.3    Marletta, M.A.4
  • 42
    • 33644818614 scopus 로고    scopus 로고
    • Thioredoxin catalyzes the S-nitrosation of the caspase-3 active site cysteine
    • Mitchell D.A., and Marletta M.A. Thioredoxin catalyzes the S-nitrosation of the caspase-3 active site cysteine. Nat. Chem. Biol. 1 (2005) 154-158
    • (2005) Nat. Chem. Biol. , vol.1 , pp. 154-158
    • Mitchell, D.A.1    Marletta, M.A.2
  • 43
    • 44449119080 scopus 로고    scopus 로고
    • Regulated protein denitrosylation by cytosolic and mitochondrial thioredoxins
    • Benhar M., Forrester M.T., Hess D.T., and Stamler J.S. Regulated protein denitrosylation by cytosolic and mitochondrial thioredoxins. Science 320 (2008) 1050-1054
    • (2008) Science , vol.320 , pp. 1050-1054
    • Benhar, M.1    Forrester, M.T.2    Hess, D.T.3    Stamler, J.S.4
  • 45
    • 0032961270 scopus 로고    scopus 로고
    • ESPript: analysis of multiple sequence alignments in PostScript
    • Gouet P., Courcelle E., Stuart D.I., and Metoz F. ESPript: analysis of multiple sequence alignments in PostScript. Bioinformatics 15 (1999) 305-308
    • (1999) Bioinformatics , vol.15 , pp. 305-308
    • Gouet, P.1    Courcelle, E.2    Stuart, D.I.3    Metoz, F.4
  • 46
    • 0027968068 scopus 로고
    • CLUSTAL W: improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice
    • Thompson J.D., Higgins D.G., and Gibson T.J. CLUSTAL W: improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice. Nucleic Acids Res. 22 (1994) 4673-4680
    • (1994) Nucleic Acids Res. , vol.22 , pp. 4673-4680
    • Thompson, J.D.1    Higgins, D.G.2    Gibson, T.J.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.