The ERO1 gene of yeast is required for oxidation of protein dithiols in the endoplasmic reticulum

Molecular Cell

Volumn 1, Issue 2, 1998, Pages 161-170

  Frand, Alison R ^a   Kaiser, Chris A ^a  

^a MASSACHUSETTS INSTITUTE OF TECHNOLOGY   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

ANTIOXIDANT; CELL SURFACE RECEPTOR; DISULFIDE; DITHIOTHREITOL; DITHIOTHREITOL TETRAACETATE; DRUG DERIVATIVE; ENZYME INHIBITOR; ERO1 PROTEIN, S CEREVISIAE; FUNGAL PROTEIN; GLUTATHIONE; GLYCOPROTEIN; PEP1 PROTEIN, S CEREVISIAE; SACCHAROMYCES CEREVISIAE PROTEIN; THIOL DERIVATIVE; VESICULAR TRANSPORT PROTEIN;

ARTICLE; CHEMISTRY; DRUG EFFECT; ENDOPLASMIC RETICULUM; ENZYMOLOGY; FUNGAL GENE; GENE EXPRESSION REGULATION; GENETICS; METABOLISM; MOLECULAR GENETICS; MUTAGENESIS; NUCLEOTIDE SEQUENCE; OXIDATION REDUCTION REACTION; PHYSIOLOGY; PROTEIN FOLDING; SACCHAROMYCES CEREVISIAE; SEQUENCE HOMOLOGY; TEMPERATURE; TRANSPORT AT THE CELLULAR LEVEL;

ANTIOXIDANTS; BIOLOGICAL TRANSPORT; CONSERVED SEQUENCE; DISULFIDES; DITHIOTHREITOL; ENDOPLASMIC RETICULUM; ENZYME INHIBITORS; FUNGAL PROTEINS; GENE EXPRESSION REGULATION, FUNGAL; GENES, FUNGAL; GLUTATHIONE; GLYCOPROTEINS; MOLECULAR SEQUENCE DATA; MUTAGENESIS; OXIDATION-REDUCTION; PROTEIN FOLDING; RECEPTORS, CELL SURFACE; SACCHAROMYCES CEREVISIAE; SACCHAROMYCES CEREVISIAE PROTEINS; SEQUENCE HOMOLOGY, AMINO ACID; SULFHYDRYL COMPOUNDS; TEMPERATURE; VESICULAR TRANSPORT PROTEINS;

EID: 0031609760     PISSN: 10972765     EISSN: None     Source Type: Journal    
DOI: 10.1016/S1097-2765(00)80017-9     Document Type: Article

References (43)

1. Bardwell, J.C.A., McGovern, K., and Beckwith, J. (1991). Identification of a protein required for disulfide bond formation in vivo. Cell 67, 581-589.
2. Bardwell, J.C.A., Lee, J.-O., Jander, G., Martin, N., Belin, D., and Beckwith, J. (1993). A pathway for disulfide bond formation in vivo. Proc. Natl. Acad. Sci. USA 90, 1038-1042.
3. Beinert, H. (1990). Recent developments in the field of iron-sulfur proteins. FASEB J. 4, 2483-2491.
4. Braakman, I., Hoover-Litty, H., Wagner, K.R., and Helenius, A. (1991). Folding of influenza hemagglutinin in the endoplasmic reticulum. J. Cell Biol. 114, 401-411.
5. Carlson, M., and Botstein, D. (1982). Two differentially regulated mRNAs with different 5′ ends encode secreted and intracellular forms of yeast invertase. Cell 28, 145-154.
6. Cherry, J.M., Adler, C., Ball, C., Dwight, S., Chervitz, S., Juvik, G., Weng, S., and Botstein, D. (1997). Saccharomyces Genome Databas (http://genome-www.stanford.edu/Saccharomyces).
7. Cox, J.S., Shamu, C.E., and Walter, P. (1993). Transcriptional induction of genes encoding endoplasmic reticulum resident proteins requires a transmembrane protein kinase. Cell 73, 1197-1206.
8. Ellis, L.B., Saurugger, P., and Woodward, C. (1992). Identification of the three-dimensional thioredoxin motif: related structure in the ORF3 protein of the Staphylococcus aureus mer operon. Biochemistry 31, 4882-4891.
9. Elrod-Erickson, M.J., and Kaiser, C.A. (1996). Genes that control the fidelity of endoplasmic reticulum to Golgi transport identified as suppressors of vesicle budding mutations. Mol. Biol. Cell 7, 1043-1058.
10. Endrizzi, J.A., Breddam, K., and Remington, S.J. (1994). 2.8-Å structure of yeast serine carboxypeptidase. Biochemistry 33, 11106-11120.
11. Espenshade, P., Gimeno, R.E., Holzmacher, E., Teung, P., and Kaiser, C.A. (1995). Yeast SEC16 gene encodes a multidomain vesicle coat protein that interacts with Sec23p. J. Cell Biol. 131, 311-324.
12. Freedman, R.B., Hirst, T.R., and Tuite, M.F. (1994). Protein disulfide isomerase: building bridges in protein folding. Trends Biochem. Sci. 19, 331-336.
13. Grant, C.M., MacIver, F.H., and Dawes, I.W. (1996). Glutathione is an essential metabolite required for resistance to oxidative stress in the yeast Saccharomyces cerevisiae. Curr. Genet. 29, 511-515.
14. Guarente, L. (1983). Yeast promoters and lacZfusions designed to study expression of cloned genes in yeast. Meth. Enzymol. 101, 181-191.
15. Guilhot, C., Jander, G., Martin, N.L., and Beckwith, J. (1995). Evidence that the pathway of disulfide bond formation in Escherichia coli involves interactions between the cysteines of DsbB and DsbA. Proc. Natl. Acad. Sci. USA 92, 9895-9899.
16. Hartwell, L.H., Mortimer, R.K., Culotti, J., and Culotti, M. (1973). Genetic control of the cell division cycle in yeast: V. Genetic analysis of cdc mutants. Genetics 74, 267-286.
17. Hong, E., Davidson, A., and Kaiser, C.A. (1996). A pathway for targeting soluble misfolded proteins to the yeast vacuole. J. Cell Biol. 135, 623-633.
18. Humphreys, D.P., Weir, N., Mountain, A., and Lund, P.A. (1995). Human protein disulfide isomerase functionally complements a dsbA mutation and enhances the yield of pectate lyase C in Escherichia coli. J. Biol. Chem. 270, 28210-28215.
19. Hwang, C., Sinskey, A.J., and Lodish, H.F. (1992). Oxidized redox state of glutathione in the endoplasmic reticulum. Science 257, 1496-1502.
20. Jämsä, E., Simonen, M., and Makarow, M. (1994).Selective retention of secretory proteins in the yeast endoplasmic reticulum by treatment of cells with reducing agent. Yeast 10, 355-370.
21. Joly, J.C., and Swartz, J.R. (1997). In vitro and in vivo redox states of the Escherichia coli periplasmic oxido reductases DsbA and DsbC. Biochemistry 36, 10067-10072.
22. Jones, J.S., and Prakash, L. (1990). Yeast Saccharomyces cerevisiae selectable markers in pUC18 polylinkers. Yeast 6, 363-366.
23. Kaiser, C., Michaelis, S., and Mitchell, A. (1994). Methods in Yeast Genetics: A Cold Spring Harbor Laboratory Course Manual (Cold Spring Harbor, NY: Cold Spring Harbor Press).
24. Kishigami, S., Kanaya, E., Kikuchi, M., and Ito, K. (1995). DsbA-DsbB interaction through their active site cysteines. J. Biol. Chem. 270, 17072-17074.
25. Kohno, K., Normington, K., Sambrook, J., Gething, M.-J., and Mori, K. (1993). The promoter region of the yeast KAR2 (BiP) gene contains a regulatory region domain that responds to the presence of unfolded proteins in the endoplasmic reticulum. Mol. Cell Biol. 13, 877-890.
26. Kosower, N.S., and Kosower, E.M. (1995). Diamide: an oxidant probe for thiols. Meth. Enzymol. 251, 123-133.
27. Laboissière, M.C., Sturley, S.L., and Raines, R.T. (1995). The essential function of protein-disulfide isomerase is to unscramble non-native disulfide bonds. J. Biol. Chem. 270, 28006-28009.
28. LaMantia, M., and Lennarz, W.J. (1993). The essential function of yeast protein disulfide isomerase does not reside in its isomerase activity. Cell 74, 899-908.
29. Lyles, M.M., and Gilbert, H.F. (1991). Catalysis of the oxidative folding of ribonuclease A by protein disulfide isomerase: dependence of the rate on the composition of the redox buffer. Biochemistry 30, 613-619.
30. Missiakas, D., Georgopoulos, C., and Raina, S. (1993). Identification and characterization of the Escherichia coli gene dsbB, whose product is involved in the formation of disulfide bonds in vivo. Proc. Natl. Acad. Sci. USA 90, 7084-7088.
31. Missiakas, D., Schwager, F., and Missiakas, D. (1995). Identification and characterization of a new disulfide isomerase-like protein (DsbD) in Escherichia coli. EMBO J. 14, 3415-3424.
32. Mori, K., Sant, A., Normington, K., Gething, M.-J. and Sambrook, J.F. (1992). A 22 bp cis acting element is necessary and sufficient for the induction of the yeast KAR2(BiP) gene by unfolded proteins. EMBO J. 11, 2583-2593.
33. Ohtake, Y., and Yabuuchi, S. (1991). Molecular cloning of the γ-glutamyl-cysteine synthetase gene of Saccharomyces cerevisiae. Yeast 7, 953-961.
34. Pollard, M.G., Travers, K.J., and Weissman, J.S. (1998). Ero1p: a novel and ubiquitous protein with an essential role in oxidative protein folding in the endoplasmic reticulum. Mol. Cell 1, this issue, 171-182.
35. Rose, M.D., Novick, P., Thomas, J.H., Botstein, D., and Fink, G.R. (1987). A Saccharomyces cerevisiae genomic plasmid bank based on a centromere-containing shuttle vector. Gene 60, 237-243.
36. Saxena, V.P., and Wetlaufer, D.B. (1970). Formation of three-dimensional structure in proteins. I. Rapid nonenzymatic reactivation of reduced lysozyme. Biochemistry 9, 5015-5022.
37. Schimmöller, F., Singer-Krüger, B., Schröder, S., Krüger, U., Barlowe, C., and Reizman, H. (1995). The absence of Emp24p, a component of ER-derived COPII-coated vesicles, causes a defect in transport of selected proteins to the Golgi. EMBO J. 14, 1329-1339.
38. Schmidt, M., Grey, M., and Brendel, M. (1996). A microbiological assay for the quantitative determination of glutathione. BioTechniques 21, 881-886.
39. Sikorski, R.S., and Hieter, P. (1989). A system of shuttle vectors and yeast host strains designed for efficient manipulation of DNA in Saccharomyces cerevisiae. Genetics 122, 19-27.
40. Sidrauski, C., Cox, J.S., and Walter, P. (1996). tRNA ligase is required for regulated mRNA splicing in the unfolded protein response. Cell 87, 405-413.
41. Simons, J.F., Ferro-Novick, S., Rose, M.D., and Helenius A. (1995). BiP/Kar2p serves as a molecular chaperone during carboxypeptidase Y folding in yeast. J. Cell Biol. 130, 41-49.
42. Tachibana, C., and Stevens, T.H. (1992). The yeast EUG1 gene encodes an endoplasmic reticulum protein that is functionally related to protein disulfide isomerase. Mol. Cell. Biol. 12, 4601-4611.
43. Tachikawa, H., Takeuchi, Y., Funahashi, W., Miura, T., Gao, X.-D., Fujimoto, D., Mizunaga, T., and Onodera, K. (1995). Isolation and characterization of a yeast gene, MPD1, the overexpression of which suppresses inviability caused by protein disulfide isomerase depletion. FEBS Lett. 369, 212-216.