Evidence for an interaction between ubiquitin-conjugating enzymes and the 26S proteasome

Molecular and Cellular Biology

Volumn 20, Issue 13, 2000, Pages 4691-4698

  Tongaonkar, Prasad ^a,b   Li, Chen ^b   Lambertson, David ^b   Ko, Bom ^b   Madura, Kiran ^b  

^a UNIVERSITY OF CALIFORNIA   (United States)

^b RUTGERS ROBERT WOOD JOHNSON MEDICAL SCHOOL   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

ENZYME; PROTEASOME; UBIQUITIN;

ARTICLE; CATALYSIS; CONJUGATION; HEAT STRESS; NONHUMAN; PRIORITY JOURNAL; PROTEIN DEGRADATION; PROTEIN INTERACTION; PROTEIN TARGETING; STRESS;

BINDING, COMPETITIVE; FUNGAL PROTEINS; HEAT; LIGASES; MULTIENZYME COMPLEXES; MUTATION; PEPTIDE HYDROLASES; PEPTIDES; PROTEASOME ENDOPEPTIDASE COMPLEX; SACCHAROMYCES CEREVISIAE PROTEINS; UBIQUITIN-CONJUGATING ENZYMES; YEASTS;

EID: 0343963701     PISSN: 02707306     EISSN: None     Source Type: Journal    
DOI: 10.1128/MCB.20.13.4691-4698.2000     Document Type: Article

References (38)

1. 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.
2. Bailly, V., S. Lauder, S. Prakash, and L. Prakash. 1997. Yeast DNA repair proteins Rad6 and Rad18 form a heterodimer that has ubiquitin conjugating, DNA binding, and ATP hydrolytic activities. J. Biol. Chem. 272:23360-23365.
3. Barhite, S., C. Thibault, and M. F. Miles. 1998. Phosducin-like protein (PhLP), a regulator of Gβγ function, interacts with the proteasomal protein SUG1. Biochim. Biophys. Acta 1402:95-101.
4. Bartel, B., I. Wunning, and A. Varshavsky. 1990. The recognition component of the N-end rule pathway. EMBO J. 9:3179-3189.
5. Chen, P., P. Johnson, T. Sommer, S. Jentsch, and M. Hochstrasser. 1993. Multiple ubiquitin-conjugating enzymes participate in the in vivo degradation of the yeast MATα2 repressor. Cell 74:357-369.
6. Coux, O., K. Tanaka, and A. L. Goldberg. 1996. Structure and functions of the 20S and 26S proteasomes. Annu. Rev. Biochem. 65:801-847.
7. Deveraux, Q., V. Ustrell, C. Pickart, and M. Rechsteiner. 1994. A 26S protease subunit that binds ubiquitin conjugates. J. Biol. Chem. 269:7059-7061.
8. Deveraux, Q., S. van Nocker, D. Mahaffey, R. Vierstra, and M. Rechsteiner. 1995. Inhibition of ubiquitin-mediated proteolysis by the Arabidopsis 26S protease suhunit S5a. J. Biol. Chem. 270:29660-29663.
9. Fujimuro, M., H. Takada, Y. Saeki, A. Toh-e, K. Tanaka, and H. Yokosawa. 1998. Growth-dependent change of the 26S proteasome in budding yeast. Biochem. Biophys. Res. Commun. 251:818-823.
10. Fujimuro, M., K. Tanaka, H. Yokosawa, and A. Toh-e. 1998. Son1p is a component of the 26S proteasome of the yeast Saccharomyces cerevisiae. FEBS Lett. 423:149-154.
11. Glickman, M. H., D. M. Rubin, O. Coux, I. Wefes, G. Pfeifer, Z. Cjeka, W. Baumeister, V. A. Fried, and D. Finley. 1998. A subcomplex of the proteasome regulatory particle required for ubiquitin-conjugate degradation and related to the COP9-signalosome and eIF3. Cell 94:615-624.
12. Glickman, M. H., D. M. Rubin, V. A. Fried, and D. Finley. 1998. The regulatory particle of the Saccharomyces cerevisiae proteasome. Mol. Cell. Biol. 18:3149-3162.
13. Hershko, A. 1991. The ubiquitin pathway for protein degradation. Trends Biochem. Sci. 16:265-268.
14. Hochstrasser, M. 1996. Ubiquitin-dependent protein degradation. Annu. Rev. Genet. 30:405-439.
15. Jentsch, S., W. Seufert, T. Sommer, and H. Reiss. 1990. Ubiquitin-conjugating enzymes: Novel regulators of eukaryotic cells. Trends Biochem. Sci. 15:195.
16. Johnson, E. S., B. Bartel, W. Seufert, and A. Varshavsky. 1992. Ubiquitin as a degradation signal. EMBO J. 11:497-505.
17. Johnson, E. S., P. C. M. Ma, I. M. Ota, and A. Varshavsky. 1995. A proteolytic pathway that recognizes ubiquitin as a degradation signal. J. Biol. Chem. 270:17442-17456.
18. Kaiser, P., V. Moncollin, D. J. Clarke, M. H. Watson, B. L. Bertolaer, S. I. Reed, and E. Bailly. 1999. Cyclin-dependent kinase and Cks/Suc1 interact with the proteasome in yeast to control proteolysis of M-phase targets. Genes Dev. 13:1190-1202.
19. Koegl, M., T. Hoppe, S. Schlenker, H. D. Ulrich, T. U. Mayer, and S. Jentsch. 1999. A novel ubiquitination factor, E4, is involved in multiubiquitin chain assembly. Cell 96:635-644.
20. Lam, Y. A., W. Xu, G. N. DeMartino, and R. E. Cohen. 1997. Editing of ubiquitin conjugates by an isopeptidase in the 26S proteasome. Nature 385: 737-740.
21. Papa, F. R., A. Y. Amerik, and M. Hochstrasser. 1999. Interaction of the Doa4 deubiquitinating enzyme with the yeast 26S proteasome. Mol. Biol. Cell 10:741-756.
22. Pickart, C. M. 1997. Targeting of substrates to the 26S proteasome. FASEB J. 11:1055-1066.
23. Ramos, P. C., J. Hockendorff, E. S. Johnson, A. Varshavsky, and R. J. Dohmen. 1998. Ump1p is required for proper maturation of the 20S proteasome and becomes its substrate upon completion of the assembly. Cell 92:489-499.
24. Robzyk, K., J. Recht, and M. A. Osley. 2000. Rad6-dependent ubiquitination of histone H2B in yeast. Science 287:501-504.
25. Schauber, C., L. Chen, P. Tongaonkar, I. Vega, D. Lambertson, W. Potts, and K. Madura. 1998. Rad23 links DNA repair to the ubiquitin/proteasome pathway. Nature 391:715-718.
26. Scheffner, M., U. Nuber, and J. M. Huibregtse. 1995. Protein ubiquitination involving an E1-E2-E3 enzyme ubiquitin thioester cascade. Nature 373:81-83.
27. 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.
28. Sung, P., E. Berleth, C. Pickart, S. Prakash, and L. Prakash. 1991. Yeast RAD6 encoded ubiquitin conjugating enzyme mediates protein degradation dependent on the N-end-recognizing E3 enzyme. EMBO J. 10:2187-2193.
29. Sung, P., S. Prakash, and L. Prakash. 1990. Mutation of cysteine-88 in the Saccharomyces cerevisiae RAD6 protein abolishes its ubiquitin-conjugating activity and its various biological functions. Proc. Natl. Acad. Sci. USA 87:2695-2699.
30. Sung, P., S. Prakash, and L. Prakash. 1988. The RAD6 protein of Saccharomyces cerevisiae polyubiquitinates histones, and its acidic domain mediates this activity. Genes Dev. 2:1476-1485.
31. Tongaonkar, P., and K. Madura. 1999. Characterization of a temperature-sensitive mutant of a ubiquitin-conjugating enzyme and its use as a heat-inducible degradation signal. Anal. Biochem. 272:263-269.
32. 32P-ubiquitin. Anal. Biochem. 260:307-319.
33. van Nocker, S., Q. Deveraux, M. Rechsteiner, and R. D. Vierstra. 1996. Arabidopsis MBP1 gene encodes a conserved ubiquitin recognition component of the 26S proteasome. Proc. Natl. Acad. Sci. USA 93:856-860.
34. van Nocker, S., S. Sadis, D. M. Rubin, M. Glickman, H. Fu, O. Coux, I. Wefes, D. Finley, and R. D. Vierstra. 1996. The multiubiquitin-chain-binding protein Mcb1 is a component of the 26S proteasome in Saccharomyces cerevisiae and plays a nonessential, substrate-specific role in protein turnover. Mol. Cell. Biol. 16:6020-6028.
35. Varshavsky, A. 1997. The ubiquitin system. Trends Biochem. Sci. 22:383-387.
36. Wang, W., P. M. Chevray, and D. Nathans. 1996. Mammalian Sug1 and c-Fos in the nuclear 26S proteasome. Proc. Natl. Acad. Sci. USA 93:8236-8240.
37. Wilkinson, K. 1997. Regulation of ubiquitin-dependent processes by deubiquitinating enzymes. FASEB J. 11:1245-1256.
38. Zhu, X., and C. M. Craft. 1998. Interaction of Phosducin and Phosducin isoforms with a 26S proteasomal subunit, SUG1. Mol. Vision 4:13.