Structural basis for the different activities of yeast Grx1 and Grx2

Biochimica et Biophysica Acta - Proteins and Proteomics

Volumn 1804, Issue 7, 2010, Pages 1542-1547

  Li, Wei Fang ^a   Yu, Jiang ^a   Ma, Xiao Xiao ^a   Teng, Yan Bin ^a   Luo, Ming ^a   Tang, Ya Jun ^a   Zhou, Cong Zhao ^a  

^a UNIVERSITY OF SCIENCE AND TECHNOLOGY OF CHINA   (China)

Author keywords

Conformational rearrangement; Crystal structure; Glutaredoxin; Glutathione; Glutathione disulfide reductase activity; Redox state

Indexed keywords

ASPARTIC ACID; GLUTAREDOXIN; GLUTAREDOXIN 1; GLUTAREDOXIN 2; GLUTATHIONE; SERINE; UNCLASSIFIED DRUG;

AMINO ACID SUBSTITUTION; ARTICLE; BINDING SITE; CRYSTAL STRUCTURE; ENZYME ACTIVITY; ENZYME METABOLISM; ENZYME STRUCTURE; PRIORITY JOURNAL; SITE DIRECTED MUTAGENESIS; STRUCTURAL HOMOLOGY; YEAST;

AMINO ACID SEQUENCE; BINDING SITES; CATALYTIC DOMAIN; CRYSTALLOGRAPHY, X-RAY; ESCHERICHIA COLI; GLUTAREDOXINS; GLUTATHIONE; MOLECULAR SEQUENCE DATA; OXIDATION-REDUCTION; OXIDATIVE STRESS; PROTEIN BINDING; PROTEIN CONFORMATION; SACCHAROMYCES CEREVISIAE PROTEINS; SEQUENCE HOMOLOGY, AMINO ACID;

EID: 77952319394     PISSN: 15709639     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbapap.2010.04.010     Document Type: Article

References (45)

1. Yu B.P. Cellular defenses against damage from reactive oxygen species. Physiol. Rev. 74 (1994) 139-162
2. Halliwell B., and Gutteridge J.M.C. Free Radicals in Biology and Medicine. 2nd edn (1989), Oxford University Press, Oxford
3. Gutteridge J.M. Free radicals in disease processes: a compilation of cause and consequence. Free radic. res. commun. 19 (1993) 141-158
4. Demple B. A bridge to control. Science 279 (1998) 1655-1656
5. Rietsch A., and Beckwith J. The genetics of disulfide bond metabolism. Annu. Rev. Genet. 32 (1998) 163-184
6. Stewart E.J., Åslund F., and Beckwith J. Disulfide bond formation in the Escherichia coli cytoplasm: an in vivo role reversal for the thioredoxins. Embo J 17 (1998) 5543-5550
7. Carmel-Harel O., and Storz G. Roles of the glutathione- and thioredoxin-dependent reduction systems in the Escherichia coli and Saccharomyces cerevisiae responses to oxidative stress. Annu. Rev. Microbiol. 54 (2000) 439-461
8. Holmgren A. Thioredoxin and glutaredoxin systems. J Biol Chem 264 (1989) 13963-13966
9. Fernandes A.P., and Holmgren A. Glutaredoxins: glutathione-dependent redox enzymes with functions far beyond a simple thioredoxin backup system. Antioxid. Redox Signal. 6 (2004) 63-74
10. Collinson E.J., and Grant C.M. Role of yeast glutaredoxins as glutathione S-transferases. J. Biol. Chem. 278 (2003) 22492-22497
11. Starke D.W., Chock P.B., and Mieyal J.J. Glutathione-thiyl radical scavenging and transferase properties of human glutaredoxin (thioltransferase). Potential role in redox signal transduction. J Biol Chem 278 (2003) 14607-14613
12. Murata H., Ihara Y., Nakamura H., Yodoi J., Sumikawa K., and Kondo T. Glutaredoxin exerts an antiapoptotic effect by regulating the redox state of Akt. J Biol Chem 278 (2003) 50226-50233
13. Song J.J., Rhee J.G., Suntharalingam M., Walsh S.A., Spitz D.R., and Lee Y.J. Role of glutaredoxin in metabolic oxidative stress. Glutaredoxin as a sensor of oxidative stress mediated by H2O2. J Biol Chem 277 (2002) 46566-46575
14. Gravina S.A., and Mieyal J.J. Thioltransferase is a specific glutathionyl mixed disulfide oxidoreductase. Biochemistry 32 (1993) 3368-3376
15. Jung C.H., and Thomas J.A. S-glutathiolated hepatocyte proteins and insulin disulfides as substrates for reduction by glutaredoxin, thioredoxin, protein disulfide isomerase, and glutathione. Arch. Biochem. Biophys. 335 (1996) 61-72
16. Gilbert H.F. Molecular and cellular aspects of thiol-disulfide exchange. Adv. Enzymol. Relat. Areas Mol. Biol. 63 (1990) 169-172
17. Thomas J.A., Poland B., and Honzatko R. Protein sulfhydryls and their role in the antioxidant function of protein S-thiolation. Arch. Biochem. Biophys. 319 (1995) 1-9
18. Eckers E., Bien M., Stroobant V., Herrmann J.M., and Deponte M. Biochemical characterization of dithiol glutaredoxin 8 from Saccharomyces cerevisiae: the catalytic redox mechanism redux (dagger). Biochemistry (2009)
19. Luikenhuis S., Perrone G., Dawes I.W., and Grant C.M. The yeast Saccharomyces cerevisiae contains two glutaredoxin genes that are required for protection against reactive oxygen species. Mol. Biol. Cell 9 (1998) 1081-1091
20. Rodriguez-Manzaneque M.T., Ros J., Cabiscol E., Sorribas A., and Herrero E. Grx5 glutaredoxin plays a central role in protection against protein oxidative damage in Saccharomyces cerevisiae. Mol. Cell. Biol. 19 (1999) 8180-8190
21. Izquierdo A., Casas C., Muhlenhoff U., Lillig C.H., and Herrero E. Saccharomyces cerevisiae Grx6 and Grx7 are monothiol glutaredoxins associated with the early secretory pathway. Eukaryot Cell 7 (2008) 1415-1426
22. Rodriguez-Manzaneque M.T., Tamarit J., Belli G., Ros J., and Herrero E. Grx5 is a mitochondrial glutaredoxin required for the activity of iron/sulfur enzymes. Mol. Biol. Cell 13 (2002) 1109-1121
23. Ojeda L., Keller G., Muhlenhoff U., Rutherford J.C., Lill R., and Winge D.R. Role of glutaredoxin-3 and glutaredoxin-4 in the iron regulation of the Aft1 transcriptional activator in Saccharomyces cerevisiae. J Biol Chem 281 (2006) 17661-17669
24. Lill R., and Muhlenhoff U. Iron-sulfur protein biogenesis in eukaryotes: components and mechanisms. Annu. Rev. Cell Dev. Biol. 22 (2006) 457-486
25. Yu J., Zhang N.N., Yin P.D., Cui P.X., and Zhou C.Z. Glutathionylation-triggered conformational changes of glutaredoxin Grx1 from the yeast Saccharomyces cerevisiae. Proteins-Struct. Funct. Bioinform. 72 (2008) 1077-1083
26. Pedrajas J.R., Porras P., Martinez-Galisteo E., Padilla C.A., Miranda-Vizuete A., and Barcena J.A. Two isoforms of Saccharomyces cerevisiae glutaredoxin 2 are expressed in vivo and localize to different subcellular compartments. Biochem. J. 364 (2002) 617-623
27. Porras P., Padilla C.A., Krayl M., Voos W., and Barcena J.A. One single in-frame AUG codon is responsible for a diversity of subcellular localizations of glutaredoxin 2 in Saccharomyces cerevisiae. J Biol Chem 281 (2006) 16551-16562
28. Bartels K., and Klein C. AUTOMAR User's Guide, v.1.4. Nov. 11, 2003 (2003). http://www.marresearch.com/automar Available at
29. Brunger A.T., Adams P.D., Clore G.M., DeLano W.L., Gros P., Grosse-Kunstleve R.W., Jiang J.S., Kuszewski J., Nilges M., Pannu N.S., Read R.J., Rice L.M., Simonson T., and Warren G.L. Crystallography & NMR system: a new software suite for macromolecular structure determination. Acta Crystallogr D 54 (1998) 905-921
30. Jones T.A., Zou J.Y., and Cowan S.W. Kjeldgaard, 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
31. Murshudov G.N., Vagin A.A., and Dodson E.J. Refinement of macromolecular structures by the maximum-likelihood method. Acta Crystallogr D 53 (1997) 240-255
32. Laskowski R.A., MacArthur M.W., Moss D.S., and Thornton J.M. PROCHECK: a program to check the stereochemical quality of protein structures. J Appl Crystallogr 26 (1993) 283-291
33. DeLano W.L. The PyMOL Molecular Graphics System (2002). http://www.pymol.org
34. Holmgren A., and Aslund F. Glutaredoxin. Methods Enzymol. 252 (1995) 283-292
35. Bacik J.P., and Hazes B. Crystal structures of a poxviral glutaredoxin in the oxidized and reduced states show redox-correlated structural changes. J Mol Biol 365 (2007) 1545-1558
36. Foloppe N., and Nilsson L. Stabilization of the catalytic thiolate in a mammalian glutaredoxin: structure, dynamics and electrostatics of reduced pig glutaredoxin and its mutants. J Mol Biol 372 (2007) 798-816
37. Moutevelis E., and Warwicker J. Prediction of pKa and redox properties in the thioredoxin superfamily. Protein Sci. 13 (2004) 2744-2752
38. Yang Y.F., and Wells W.W. Identification and characterization of the functional amino acids at the active center of pig liver thioltransferase by site-directed mutagenesis. J Biol Chem 266 (1991) 12759-12765
39. Discola K.F., de Oliveira M.A., Rosa Cussiol J.R., Monteiro G., Barcena J.A., Porras P., Padilla C.A., Guimaraes B.G., and Netto L.E. Structural aspects of the distinct biochemical properties of glutaredoxin 1 and glutaredoxin 2 from Saccharomyces cerevisiae. J Mol Biol 385 (2009) 889-901
40. Lillig C.H., Berndt C., and Holmgren A. Glutaredoxin systems. Biochim. Biophys. Acta 1780 (2008) 1304-1317
41. Sagemark J., Elgan T.H., Burglin T.R., Johansson C., Holmgren A., and Berndt K.D. Redox properties and evolution of human glutaredoxins. Proteins 68 (2007) 879-892
42. Mesecke N., Spang A., Deponte M., and Herrmann J.M. A novel group of glutaredoxins in the cis-Golgi critical for oxidative stress resistance. Mol. Biol. Cell 19 (2008) 2673-2680
43. Corpet F. Multiple sequence alignment with hierarchical clustering. Nucleic Acids Res. 16 (1988) 10881-10890
44. Gouet P., Robert X., and Courcelle E. ESPript/ENDscript: extracting and rendering sequence and 3D information from atomic structures of proteins. Nucleic Acids Res. 31 (2003) 3320-3323
45. Kabsch W., and Sander C. Dictionary of protein secondary structure: pattern recognition of hydrogen-bonded and geometrical features. Biopolymers 22 (1983) 2577-2637