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

Molecular and Cellular Biology

Volumn 16, Issue 11, 1996, Pages 6020-6028

  Van Nocker, Steven ^a   Sadis, Seth ^b   Rubin, David M ^b   Glickman, Michael ^b   Fu, Hongyong ^a   Coux, Olivier ^b   Wefes, Inge ^b   Finley, Daniel ^b   Vierstra, Richard D ^a  

^a UNIVERSITY OF WISCONSIN MADISON   (United States)

^b HARVARD MEDICAL SCHOOL   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

AMINO ACID; AMINO ACID DERIVATIVE; BETA GALACTOSIDASE; BINDING PROTEIN; NICKEL; PROTEASOME; UBIQUITIN;

AMINO ACID SEQUENCE; ARTICLE; CHROMATOGRAPHY; ENZYME SPECIFICITY; GENE; IMMUNOBLOTTING; NONHUMAN; POLYMERASE CHAIN REACTION; PRIORITY JOURNAL; PROTEIN DEGRADATION; PROTEIN METABOLISM; SACCHAROMYCES CEREVISIAE; SEQUENCE HOMOLOGY;

ANIMALIA; SACCHAROMYCES CEREVISIAE;

EID: 0029806477     PISSN: 02707306     EISSN: None     Source Type: Journal    
DOI: 10.1128/MCB.16.11.6020     Document Type: Article

References (54)

1. Arnason, T., and M. J. Ellison. 1994. Stress resistance in Saccharomyces cerevisiae is strongly correlated with assembly of a novel type of multiubiquitin chain. Mol. Cell. Biol. 14:7876-7883.
2. EPF and RAD6 are recognized by 26S proteasome subunit 5. J. Biol. Chem. 271:2823-2831.
3. 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.
4. Bartel, B., I. Wünning, and A. Varshavsky. 1990. The recognition component of the N-end rule pathway. EMBO J. 9:3179-3189.
5. Beale, R., Q. Deveraux, G. Xia, M. Rechsteiner, and C. Pickart. 1996. Surface hydrophobic residues of multiubiquitin chains essential for proteolytic targeting. Proc. Natl. Acad Sci. USA 93:861-866.
6. Chau, V., J. W. Tobias, A. Bachmair, D. Marriott, D. J. Ecker, D. K. Gonda, and A. Varshavsky. 1989. A multiubiquitin chain is confined to a specific lysine in a targeted short-lived protein. Science 243:1576-1583.
7. Ciechanover, A. 1994. The ubiquitin-proteasome proteolytic pathway. Cell 79:13-21.
8. Cook, W. J., L. C. Jeffrey, E. Kasperek, and C. M. Pickart. 1994. Structure of tetraubiquitin shows how multiubiquitin chains can be formed. J. Mol. Biol. 236:601-609.
9. DeMartino, G. N., R. J. Proske, C. R. Moomaw, A. A. Strong, X. L. Song, H. Hisamatsu, K. Tanaka, and C. A. Slaughter. 1996. Identification, purification, and characterization of a PA700-dependent activator of the proteasome. J. Biol. Chem. 271:3112-3118.
10. Deveraux, Q., V. Ustrell, C. Piekart, and M. Rechsteiner. 1994. A 26S protease subunit that binds ubiquitin conjugates. J. Biol. Chem. 269:7059-7061.
11. Deveraux, Q., S. van Nocker, D. Mahaffey, R. D. Vierstra, and M. Rechsteiner. 1995. Inhibition of ubiquitin-mediated proteolysis by the Arabidopsis 26S protease subunit AtMbp1. J. Biol. Chem. 270:29660-29663.
12. Devereux, J., P. Haeberli, and O. Smithies. 1984. A comprehensive set of sequence analysis programs for the VAX. Nucleic Acids Res. 12:387-395.
13. 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.
14. Ferrell, K., Q. Deveraux, S. van Nocker, and M. Rechsteiner. 1996. Molecular cloning and expression of a multiubiquitin chain binding subunit of the human 26S protease. FEBS Lett. 381:143-148.
15. Finley, D., E. Özkaynak, and A. Varshavsky. 1987. The yeast polyubiquitin gene is essential for resistance to high temperature, starvation, and other stresses. Cell 48:1035-1046.
16. Finley, D., S. Sadis, B. P. Monia, P. Boucher, D. J. Ecker, S. T. Crooke, and V. Chau. 1994. Inhibition of proteolysis and cell cycle progression in a multiubiquitination-deficient yeast mutant. Mol. Cell. Biol. 14:5501-5509.
17. 16a. Fu, H., and R. D. Vierstra. Unpublished data.
18. Ghislain, M., A. Udvardy, and C. Mann. 1993. S. cerevisiae 26S protease mutants arrest cell division in G2/metaphase. Nature (London) 366:358-362.
19. Gietz, R. D., R. H. Schiestl, A. R. Willems, and R. A. Woods. 1995. Studies on the transformation of intact yeast cells by the LiAc/SS-DNA/PEG procedure. Yeast 11:355-360.
20. Glotzer, M., A. W. Murray, and M. W. Kirschner. 1991. Cyclin is degraded by the ubiquitin pathway. Nature (London) 349:132-138.
21. Haracska, L., and A. Udvardy. 1995. Cloning and sequencing a non-ATPase subunit of the regulatory complex of the Drosophila 26S protease. Eur. J. Biochem. 231:720-725.
22. Heinemeyer, W., A. Gruhler, V. Möhrle, Y. Mahé, and D. H. Wolf. 1993. PRE2, highly homologous to the human major histocompatibility complex-linked Ring10 gene, codes for a yeast proteasome unit necessary for chymotryptic activity and degradation of ubiquitinated proteins. J. Biol. Chem. 268:5115-5120.
23. Heinemeyer, W., N. Trondle, G. Albrecht, and D. H. Wolf. 1994. PRE5 and PRE6. the last missing genes encoding 20S proteasome subunits from yeast? Indication for a set of 14 different subunits in the eukaryotic proteasome core. Biochemistry 33:12229-12237.
24. Hershko, A., and A. Ciechanover. 1992. The ubiquitin system for protein degradation. Annu. Rev. Biochem. 61:761-807.
25. Hicke, L., and H. Riezman. 1996. Ubiquitination of a yeast plasma membrane receptor signals its ligand-stimulated endocytosis. Cell 84:277-287.
26. Hochstrasser, M., M. J. Ellison, V. Chau, and A. Varshavsky. 1991. The short-lived MATα2 transcriptional regulator is ubiquitinated in vivo. Proc. Natl. Acad. Sci. USA 88:4606-4610.
27. Hofmann, K. 1995. BoxShade 2.7. Published electronically. Available by anonymous FTP from vax0.biomed.uni-koeln.de.
28. Jabben, M., J. Shanklin, and R. D. Vierstra. 1989. Ubiquitin-phytochrome conjugates: pool dynamics during in vivo phytochrome degradation. J. Biol. Chem. 264:4998-5005.
29. Jentsch, S. 1992. The ubiquitin-conjugation system. Annu. Rev. Genet. 26: 179-207.
30. Johansson, E., I. Lönnroth, S. Lange, I. Honson, E. Jennische, and C. Lönnroth. 1995. Molecular cloning and expression of a pituitary gland protein modulating intestinal fluid secretion. J. Biol. Chem. 270:20615-20620.
31. 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.
32. Johnston, M., S. Andrew, R. Brinkman, J. Cooper, H. Ding, et al. 1994. The complete nucleotide sequence of Saccharomyces cerevisiae chromosome VIII. Science 265:2077-2082.
33. Kornitzer, D., B. Raboy, R. G. Kulka, and G. R. Fink. 1994. Regulated degradation of the transcription factor Gcn4. EMBO J. 13:6021-6030.
34. Madura, K., and A. Varshavsky. 1994. Degradation of Gα by the N-end rule pathway. Science 265:1454-1458.
35. 2 in Mos. EMBO J. 12:4021-4027.
36. Palombella, V. J., O. J. Rando, A. L. Goldberg, and T. Maniatis. 1994. The ubiquitin-proteasome pathway is required for processing the NF-κB1 precursor protein and the activation of NF-κB. Cell 78:773-785.
37. Papa, F. R. Personal communication.
38. Papa, F. R., and M. Hochstrasser. 1993. The yeast DOA4 gene encodes a deubiquitinating enzyme related to the product of the human tre-2 oncogene. Nature (London) 366:313-319.
39. Peters, J. M., W. W. Franke, and J. A. Kleinschmidt. 1994. Distinct 19S and 20S subcomplexes of the 26S proteasome and their distribution in the nucleus and cytoplasm. J. Biol. Chem. 269:7709-7718.
40. Rechsteiner, M., L. Hoffman, and W. Dubiel. 1993. The multicatalytic and 26S proteases. J. Biol. Chem. 268:6065-6068.
41. Rose, M. D., F. Winston, and P. Hieter. 1990. Methods in yeast genetics. Cold Spring Harbor Laboratory Press, Cold Spring Harbor, N.Y.
42. Rubin, D. M., O. Coux, I. Wefes, C. Hengartner, M. Ghislain, R. A. Young, A. L. Goldberg, and D. Finley. 1996. Identification of the gal4 suppressor Sug1 as a subunit of the yeast 26S proteasome. Nature (London) 379:655-657.
43. Rubin, D. M., and D. Finley. 1995. The proteasome: a protein-degrading organelle? Curr. Biol. 5:854-858.
44. Sambrook, J., E. F. Fritsch, and T. Maniatis. 1989. Molecular cloning: a laboratory manual. 2nd ed. Cold Spring Harbor Laboratory Press, Cold Spring Harbor, N.Y.
45. Scheffner, M., J. M. Huibregtse, R. D. Vierstra, and P. M. Howley. 1993. The HPV-16 E6 and E6-AP complex functions as a ubiquitin-protein ligase in ubiquitination of p53. Cell 75:495-505.
46. 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.
47. Seufert, W., and S. Jentsch. 1992. In vivo function of the proteasome in the ubiquitin pathway. EMBO J. 11:3077-3080.
48. Sikorski, R. S., and P. Hieter. 1989. A system of shuttle vectors and yeast host strains designed for efficient manipulation of DNA in Saccharomyces cerevisiae. Genetics 122:19-27.
49. Spence, J., S. Sadis, A. L. Haas, and D. Finley. 1995. A ubiquitin mutant with specific defects in DNA repair and multiubiquitination. Mol. Cell. Biol. 15:1265-1273.
50. Tanahashi, N., C. Tsurumi, T. Tamura, and K. Tanaka. 1993. Molecular structures of the 20S and 26S proteasomes. Enzyme Protein 47:241-251.
51. Treier, M., L. M. Staszewski, and D. Bohmann. 1994. Ubiquitin-dependent c-jun degradation in vivo is mediated by the δ domain. Cell 78:787-798.
52. 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.
53. van Nocker, S., and R. D. Vierstra. 1993. Multiubiquitin chains linked through Lysine 48 are abundant in vivo and are competent intermediates in the ubiquitin proteolytic pathway. J. Biol. Chem. 268:24766-24773.
54. Wurst, H., T. Shiba, and A. Kornberg. 1995. The gene for a major exopolyphosphatase of Saccharomyces cerevisiae. J. Bacteriol. 177:898-906.