Involvement of the molecular chaperone Ydj1 in the ubiquitin-dependent degradation of short-lived and abnormal proteins in Saccharomyces cerevisiae

Molecular and Cellular Biology

Volumn 16, Issue 9, 1996, Pages 4773-4781

  Lee, Do Hee ^a   Sherman, Michael Y ^b   Goldberg, Alfred L ^a  

^a HARVARD MEDICAL SCHOOL   (United States)

^b BOSTON BIOMEDICAL RESEARCH INSTITUTE   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

CHAPERONE; HYBRID PROTEIN; POLYPEPTIDE; PROTEASOME; UBIQUITIN;

AMINO ACID SEQUENCE; ARTICLE; ENZYME ACTIVITY; ENZYME SUBSTRATE; FUNGUS CULTURE; NONHUMAN; PEPTIDE ANALYSIS; PRIORITY JOURNAL; PROTEIN DEGRADATION; PROTEIN METABOLISM; SACCHAROMYCES CEREVISIAE; TEMPERATURE SENSITIVE MUTANT; YEAST;

ESCHERICHIA COLI; FUNGI; SACCHAROMYCES CEREVISIAE;

EID: 0001389495     PISSN: 02707306     EISSN: None     Source Type: Journal    
DOI: 10.1128/MCB.16.9.4773     Document Type: Article

References (42)

1. Ausubel, F. M., R. Brent, R. E. Kingston, D. D. Moore, J. G. Seidman, J. A. Smith, and K. Struhl. 1987. Current protocols in molecular biology. Wiley Interscience, New York.
2. Bachmair, A., D. Finley, and A. Varshavsky. 1986. In vivo half-life of a protein is a function of its amino-terminal residue. Science 234:179-186.
3. Caplan, A. J., D. M. Cyr, and M. G. Douglas. 1992. Ydj1p facilitates polypeptide translocation across different intracellular membranes by a conserved mechanism. Cell 71:1143-1155.
4. Chirico, W., M. G. Walter, and G. Blobel. 1988. 70K heat shock related proteins stimulate protein translocation into microsomes. Nature (London) 332:805-810.
5. Ciechanover, A. 1995. The ubiquitin-proteasome proteolytic pathway. Cell 79:13-21.
6. Craig, E. A., B. D. Ganabil, and R. J. Nelson. 1993. Heat shock proteins: molecular chaperones of protein biogenesis. Microbiol. Rev. 57:402-414.
7. Cyr, D. M., T. Langer, and M. G. Douglas. 1994. DnaJ-like proteins: molecular chaperones and specific regulators of hsp70. Trends Biochem. Sci. 19:176-181.
8. Cyr, D. M., X. Lu, and M. G. Douglas. 1992. Regulation of eukaryotic hsp70 function by a dnaJ homolog. J. Biol. Chem. 267:20927-20931.
9. Deshaies, R. J., B. D. Koch, M. Wemer-Washburne, E. A. Craig, and R. Schekman. 1988. A subfamily of hsp proteins facilitates translocation of secretory and mitochondrial precursor polypeptides. Nature (London) 332: 800-805.
10. Dohmen, R. J., K. Madura, B. Bartel, and A. Varshavsky. 1991. The N-end rule is mediated by the Ubc2 (Rad6) ubiquitin-conjugating enzyme. Proc. Natl. Acad. Sci. USA 88:7351-7355.
11. Figueiredo-Pereira, M. E., K. A. Berg, and S. Wilk. 1994. A new inhibitor of the chymotrypsin-like activity of the multicatalytic proteinase complex (20S proteasome) induces accumulation of ubiquitin-protein conjugates in a neuronal cell. J. Neurochem. 63:1578-1581.
12. Georgopoulos, C., and W. J. Welch. 1993. Role of the major heat shock proteins as molecular chaperones. Annu. Rev. Cell Biol. 9:601-634.
13. Goldberg, A. L. 1995. Functions of the proteasome: the lysis at the end of the tunnel. Science 268:522-523.
14. Goldberg, A. L., and A. C. St. John. 1976. Intracellular protein degradation in mammalian and bacterial cells. Annu. Rev. Biochem. 45:747-803.
15. Gragerov, A., E. Nudler, N. Komissarova, G. A. Gaitanaris, M. E. Gottesman, and V. Nikiforov. 1992. Cooperation of groEL/ES and DnaK/DnaJ heat shock proteins in preventing protein misfolding in Escherichia coli. Proc. Natl. Acad. Sci. USA 89:10341-10344.
16. Heinemeyer, W., A. Gruhler, V. Mohrle, Y. Mahe, and D. H. Wolf. 1993. PRE2, highly homologous to the human major histocompatibility complex-linked RING10 gene, codes for a yeast proteasome subunit necessary for chymotryptic activity and degradation of ubiquitinated proteins. J. Biol. Chem. 268:5115-5120.
17. Hendricks, J. P., and F.-U. Hartl. 1993. Molecular chaperone functions of heat shock proteins. Annu. Rev. Biochem. 62:349-384.
18. Hershko, A., and A. Ciechanover. 1992. The ubiquitin system for protein degradation. Annu. Rev. Biochem. 61:761-807.
19. 18a. Hohfeld, J., Y. Minami, and F.-U. Hartl. 1995. Hip, a novel cochaperone involved in the eukaryotic hsc70/hsp40 reaction cycle. Cell 83:589-598.
20. Jentsch, S. 1992. The ubiquitin-conjugation system. Annu. Rev. Genet. 26: 179-207.
21. Johnson, E. S., B. Bartel, W. Seufert, and A. Varshavsky. 1992. Ubiquitin as a degradation signal. EMBO J. 11:497-505.
22. Jones, E. W. 1991. Three proteolytic systems in the yeast Saccharomyces cerevisiae. J. Biol. Chem. 266:7963-7966.
23. Kandror, O., L. Busconi, M. Y. Sherman, and A, L. Goldberg. 1994. Rapid degradation of an abnormal protein in Escherichia coli involves the chaperones GroEL and GroES. J. Biol. Chem. 269:23575-23582.
24. Knittler, M. R., S. Dirks, and I. G. Haas. 1995. Molecular chaperones involved in protein degradation in the endoplasmic reticulum: quantitative interaction of the heat shock cognate protein BiP with partially folded immunoglobulin light chain that are degraded in the endoplasmic reticulum. Proc. Natl. Acad. Sci. USA 92:1764-1768.
25. Kornitzer, D., B. Raboy, R. G. Kulka, and G. R. Fink. 1994. Regulated degradation of the transcription factor Gcn4. EMBO J. 13:6021-6030.
26. Lee, D. H., and A. L. Goldberg. Unpublished data.
27. Lee, D. H., M. Y. Sherman, and A. L. Goldberg. Unpublished data.
28. Pratt, G., R. Hough, and M. Rechsteiner. 1989. Proteolysis in heat-stressed HeLa cells. J. Biol. Chem. 264:12526-12532.
29. Rechsteiner, M., L. Hoffman, and W. Dubiel. 1993. The multicatalytic and 26S proteases. J. Biol. Chem. 268:6065-6068.
30. Rose, M. D., F. Winston, and P. Hieter. 1990. Methods in yeast genetics: a laboratory course manual. Cold Spring Harbor Laboratory, Cold Spring Harbor, N.Y.
31. Seufert, W., B. Futcher, and S. Jentsch. 1995. Role of a ubiquitin-conjugating enzyme in degradation of S- and M-phase cyclins. Nature (London) 373:78-81.
32. Seufert, W., and S. Jentsch. 1990. Ubiquitin-conjugating enzymes UBC4 and UBC5 mediate selective degradation of short-lived and abnormal proteins. EMBO J. 9:543-550.
33. Sherman, M. Y., and A. L. Goldberg. 1992. Involvement of chaperonin dnaK in the rapid degradation of a mutant protein in Escherichia coli. EMBO J. 11:71-77.
34. Sherman, M. Y., and A. L. Goldberg. Involvement of molecular chaperones in intracellular breakdown. In U. Feige, R. I. Morimoto, I. Yahara, and B. S. PoIIa (ed.), Stress-inducible cellular responses, in press. Birkhäuser/Springer.
35. Straus, D. B., W. A. Walter, and C. A. Gross. 1988. Escherichia coli heat shock gene mutants are defective in proteolysis. Genes Dev. 2:1851-1858.
36. Straus, D. B., W. A. Watter, and C. A. Gross. 1990. DnaK, dnaJ and grpE heat shock proteins negatively regulate heat shock gene expression by controlling the synthesis and stability of sigma 32. Genes Dev. 4:2202-2209.
37. Tilly, K., J. Spence, and C. Georgopoulos. 1989. Modulation of stability of the Escherichia coli heat shock regulatory factor sigma. J. Bacteriol. 171: 1585-1589.
38. Varshavsky, A. 1992. The N-end rule. Cell 69:725-735.
39. Wagner, I., H. Arit, L. van Dyck, T. Langer, and W. Neupert. 1994. Molecular chaperones cooperate with pim1 protease in the degradation of misfolded proteins in mitochondria. EMBO J. 13:5135-5145.
40. Wild, J., E. Altman, T. Yura, and C. A. Gross. 1992. DnaK and DnaJ heat shock proteins participate in protein export in Escherichia coli. Genes Dev. 6:1165-1172.
41. cdc28-dependent phosphorylation of the cyclin Cln3 that signals its degradation. Mol. Cell. Biol. 16: 3679-3684.
42. Zhong, T., and K. T. Arndt. 1993. The yeast Sis1 protein, a DnaJ homolog, is required for the initiation of translation. Cell 73:1175-1186.