Two endoplasmic reticulum PDI peroxidases increase the efficiency of the use of peroxide during disulfide bond formation

Journal of Molecular Biology

Volumn 406, Issue 3, 2011, Pages 503-515

  Nguyen, Van Dat ^a   Saaranen, Mirva J ^a   Karala, Anna Riikka ^a   Lappi, Anna Kaisa ^a   Wang, Lei ^b   Raykhel, Irina B ^a   Alanen, Heli I ^a   Salo, Kirsi E H ^a   Wang, Chih Chen ^b   Ruddock, Lloyd W ^a  

^a UNIVERSITY OF OULU   (Finland)

^b INSTITUTE OF GEOLOGY AND GEOPHYSICS   (China)

Author keywords

glutathione peroxidase; hydrogen peroxide; oxidative protein folding; protein disulfide isomerase; thioredoxin fold

Indexed keywords

GLUTATHIONE PEROXIDASE; GLUTATHIONE PEROXIDASE 7; GLUTATHIONE PEROXIDASE 8; MEMBRANE PROTEIN; OXYGEN; PDI PEROXIDASE; PEROXIDASE; PEROXIDE; PROTEIN DISULFIDE ISOMERASE; PROTEIN ERO1ALPHA; UNCLASSIFIED DRUG;

ARTICLE; CONTROLLED STUDY; DISULFIDE BOND; ENDOPLASMIC RETICULUM; FLOW KINETICS; HUMAN; IN VITRO STUDY; IN VIVO STUDY; OXIDATIVE PHOSPHORYLATION; OXYGEN CONSUMPTION; PEROXIDATION; PRIORITY JOURNAL; PROTEIN DENATURATION; PROTEIN FOLDING; PROTEIN PROTEIN INTERACTION;

EID: 79551689187     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jmb.2010.12.039     Document Type: Article

References (36)

1. Thorpe C., and Coppock D.L. Generating disulfides in multicellular organisms: emerging roles for a new flavoprotein family J. Biol. Chem. 282 2007 13929 13933
2. Gross E., Sevier C.S., Heldman N., Vitu E., Bentzur M., and Kaiser C.A. Generating disulfides enzymatically: reaction products and electron acceptors of the endoplasmic reticulum thiol oxidase Ero1p Proc. Natl Acad. Sci. USA 103 2006 299 304
3. Enyedi B., Várnai P., and Geiszt M. Redox state of the endoplasmic reticulum is controlled by Ero1L-α and intraluminal calcium Antioxid. Redox Signal. 13 2010 721 729
4. Appenzeller-Herzog C., Riemer J., Christensen B., Sørensen E.S., and Ellgaard L. A novel disulphide switch mechanism in Ero1α balances ER oxidation in human cells EMBO J. 27 2008 2977 2987
5. Baker K.M., Chakravarthi S., Langton K.P., Sheppard A.M., Lu H., and Bulleid N.J. Low reduction potential of Ero1α regulatory disulphides ensures tight control of substrate oxidation EMBO J. 27 2008 2988 2997
6. Karala A.R., Lappi A.K., Saaranen M.J., and Ruddock L.W. Efficient peroxide mediated oxidative refolding of a protein at physiological pH and implications for oxidative folding in the endoplasmic reticulum Antioxid. Redox Signal. 11 2009 963 970
7. Mills G.C. Hemoglobin catabolism. Glutathione peroxidase, an erythrocyte enzyme which protects hemoglobin from oxidative breakdown J. Biol. Chem. 229 1957 189 197
8. Toppo S., Vanin S., Bosello V., and Tosatto S.C. Evolutionary and structural insights into the multifaceted glutathione peroxidase (GPx) superfamily Antioxid. Redox Signal. 10 2008 1501 1514
9. Toppo S., Floché L., Ursini F., Vanin S., and Maiorino M. Catalytic mechanisms and specificities of glutathione peroxidases: variations of a basic scheme Biochim. Biophys. Acta 1790 2009 1486 1500
10. Herbette S., Roeckel-Drevet P., and Drevet J.R. Seleno-independent glutathione peroxidases more than just simple antioxidant scavengers FEBS J. 274 2007 2163 2180
11. Hatahet F., and Ruddock L.W. Protein disulfide isomerase: a critical evaluation of its function in disulfide bond formation Antioxid. Redox Signal. 11 2009 2807 2850
12. Raykhel I., Alanen H., Salo K., Jurvansuu J., Nguyen V.D., Latva-Ranta M., and Ruddock L. A molecular specificity code for the three mammalian KDEL receptors J. Cell Biol. 179 2007 1193 1204
13. Utomo A., Jiang X., Furuta S., Yun J., Levin D.S., and Wang Y.C.J. Identification of a novel putative non-selenocysteine containing phospholipid hydroperoxide glutathione peroxidase (NPGPx) essential for alleviating oxidative stress generated from polyunsaturated fatty acids in breast cancer cells J. Biol. Chem. 279 2004 43522 43529
14. Paglia D.E., and Valentine W.N. Studies on the quantitative and qualitative characterization of erythrocyte glutathione peroxidase J. Lab. Clin. Med. 70 1967 158 169
15. Darby N.J., and Creighton T.E. Characterization of the active site cysteine residues of the thioredoxin-like domains of protein disulfide isomerase Biochemistry 34 1995 16770 16780
16. Linster C.L., and Van Schaftingen E. Vitamin C. Biosynthesis, recycling and degradation in mammals FEBS J. 274 2007 1 22
17. Alanen H.I., Williamson R.A., Howard M.J., Hatahet F.S., Salo K.E., and Kauppila A. ERp27, a new non-catalytic endoplasmic reticulum located human PDI-family member, interacts with ERp57 J. Biol. Chem. 281 2006 33727 33738
18. Malhotra J.D., Miao H., Zhang K., Wolfson A., Pennathur S., Pipe S.W., and Kaufman R.J. Antioxidants reduce endoplasmic reticulum stress and improve protein secretion Proc. Natl Acad. Sci. USA 105 2008 18525 18530
19. Tavender T.J., Sheppard A.M., and Bulleid N.J. Peroxiredoxin IV is an endoplasmic reticulum localized enzyme forming oligomeric complexes in human cells Biochem. J. 411 2008 191 199
20. 2 produced during disulphide formation J. Cell Sci. 123 2010 2672 2679
21. Zito E., Melo E.P., Yang Y., Wahlander Å., Neubert T.A., and Ron D. Oxidative protein folding by an endoplasmic reticulum-localized peroxiredoxin Mol. Cell 40 2010 787 797
22. Tavender T.J., Springate J.J., and Bulleid N.J. Recycling of peroxiredoxin IV provides a novel pathway for disulphide formation in the endoplasmic reticulum EMBO J. 29 2010 4185 4197
23. Jessop C.E., Watkins R.H., Simmons J.J., Tasab M., and Bulleid N. Protein disulphide isomerase family members show distinct substrate specificity: P5 is targeted to BiP client proteins J. Cell Sci. 122 2009 4287 4295
24. Alanen H.I., Salo K.E.H., Pekkala M., Siekkinen H.M., Pirneskoski A., and Ruddock L.W. Defining the domain boundaries of the human protein disulphide isomerases Antioxid. Redox Signal. 5 2003 367 374
25. Karala A.R., and Ruddock L.W. Does S-methyl methanethiosulfonate trap the thiol-disulphide state of proteins? Antioxid. Redox Signal. 9 2007 527 531
26. Nyfeler B., Michnick S.W., and Hauri H.P. Capturing protein interactions in the secretory pathway of living cells Proc. Natl Acad. Sci. USA 102 2005 6350 6355
27. Griesbeck O., Baird G.S., Campbell R.E., Zacharias D.A., and Tsien R.Y. Reducing the environmental sensitivity of yellow fluorescent protein. Mechanism and applications J. Biol. Chem. 276 2001 29188 29194
28. Olivari S., Galli C., Alanen H., Ruddock L., and Molinari M. A novel stress-induced EDEM variant regulating ER-associated glycoprotein degradation J. Biol. Chem. 280 2005 2424 2428
29. Lappi A.K., Lensink M.F., Alanen H.I., Salo K.E., Lobell M., Juffer A.H., and Ruddock L.W. A conserved arginine plays a role in the catalytic cycle of the protein disulphide isomerases J. Mol. Biol. 335 2004 283 295
30. Karala A., Psarrakos P., Ruddock L.W., and Klappa P. Protein disulphide isomerases from C. elegans are equally efficient at thiol-disulphide exchange in simple peptide based systems but show differences in their reactivity towards protein substrates Antioxid. Redox Signal. 9 2007 1815 1824
31. Wang L., Li S.J., Sidhu A., Zhu L., Liang Y., Freedman R.B., and Wang C.C. Reconstitution of human Ero1-Lα/protein-disulfide isomerase oxidative folding pathway in vitro. Position-dependent differences in role between the a and a′ domains of protein-disulfide isomerase J. Biol. Chem. 284 2009 199 206
32. Horecker B.L., and Kornberg A. The extinction coefficients of the reduced band of pyridine nucleotides J. Biol. Chem. 175 1948 385 390
33. Kursula P. XDSi: a graphical interface for the data processing program XDS J. Appl. Crystallogr. 37 2004 347 348
34. Schwarzenbacher R., Godzik A., Grzechnik S.K., and Jaroszewski L. The importance of alignment accuracy for molecular replacement Acta Crystallogr., Sect. D: Biol. Crystallogr. 60 2004 1229 1236
35. Emsley P., and Cowtan K. Coot: model-building tools for molecular graphics Acta Crystallogr., Sect. D: Biol. Crystallogr. 60 2004 2126 2132
36. Murshudov A., Vagin A., and Dodson E.J. Refinement of macromolecular structures by the maximum-likelihood method Acta Crystallogr., Sect. D: Biol. Crystallogr. 53 1997 240 255