A multimeric assembly factor controls the formation of alternative 20S proteasomes

Nature Structural and Molecular Biology

Volumn 15, Issue 3, 2008, Pages 237-244

  Kusmierczyk, Andrew R ^a   Kunjappu, Mary J ^a   Funakoshi, Minoru ^a   Hochstrasser, Mark ^a  

^a YALE UNIVERSITY   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

FUNGAL PROTEIN; PROTEIN PBA3; PROTEIN PBA4; PROTEIN SUBUNIT; CHAPERONE; DMP1 PROTEIN, S CEREVISIAE; DMP2 PROTEIN, S CEREVISIAE; HEAVY METAL; MULTIENZYME COMPLEX; MUTANT PROTEIN; PROTEASOME; SACCHAROMYCES CEREVISIAE PROTEIN; UNCLASSIFIED DRUG;

ARTICLE; BIOGENESIS; CELL GROWTH; COMPLEX FORMATION; CONTROLLED STUDY; NONHUMAN; PRIORITY JOURNAL; PROTEIN ASSEMBLY; PROTEIN BINDING; PROTEIN DEPLETION; PROTEIN FUNCTION; PROTEIN PROTEIN INTERACTION; SACCHAROMYCES CEREVISIAE; SEQUENCE ANALYSIS; STOICHIOMETRY; BIOLOGICAL MODEL; BIOLOGY; CHEMISTRY; CYTOLOGY; DRUG EFFECT; ENZYMOLOGY; GENETICS; GROWTH, DEVELOPMENT AND AGING; METABOLISM; MUTATION; PROTEIN SECONDARY STRUCTURE;

EUKARYOTA;

COMPUTATIONAL BIOLOGY; METALS, HEAVY; MODELS, BIOLOGICAL; MOLECULAR CHAPERONES; MULTIENZYME COMPLEXES; MUTANT PROTEINS; MUTATION; PROTEASOME ENDOPEPTIDASE COMPLEX; PROTEIN BINDING; PROTEIN STRUCTURE, SECONDARY; PROTEIN SUBUNITS; SACCHAROMYCES CEREVISIAE; SACCHAROMYCES CEREVISIAE PROTEINS;

EID: 40949117574     PISSN: 15459993     EISSN: 15459985     Source Type: Journal    
DOI: 10.1038/nsmb.1389     Document Type: Article

References (37)

1. Hochstrasser, M. Ubiquitin-dependent protein degradation. Annu. Rev. Genet. 30, 405-439 (1996).
2. Glickman, M.H. & Ciechanover, A. The ubiquitin-proteasome proteolytic pathway: destruction for the sake of construction. Physiol. Rev. 82, 373-428 (2002).
3. DeMartino, G.N. & Slaughter, C.A. The proteasome, a novel protease regulated by multiple mechanisms. J. Biol. Chem. 274, 22123-22126 (1999).
4. Heinemeyer, W., Ramos, P.C. & Dohmen, R.J. The ultimate nanoscale mincer: assembly, structure and active sites of the 20S proteasome core. Cell. Mol. Life Sci. 61, 1562-1578 (2004).
5. Chen, P. & Hochstrasser, M. Autocatalytic subunit processing couples active site formation in the 20S proteasome to completion of assembly. Cell 86, 961-972 (1996).
6. Arendt, C.S. & Hochstrasser, M. Identification of the yeast 20S proteasome catalytic centers and subunit interactions required for active-site formation. Proc. Natl. Acad. Sci. USA 94, 7156-7161 (1997).
7. Heinemeyer, W., Fischer, M., Krimmer, T., Stachon, U. & Wolf, D.H. The active sites of the eukaryotic 20 S proteasome and their involvement in subunit precursor processing. J. Biol. Chem. 272, 25200-25209 (1997).
8. Kruger, E., Kloetzel, P.M. & Enenkel, C. 20S proteasome biogenesis. Biochimie 83, 289-293 (2001).
9. Hirano, Y. et al. A heterodimeric complex that promotes the assembly of mammalian 20S proteasomes. Nature 437, 1381-1385 (2005).
10. Nandi, D., Woodward, E., Ginsburg, D.B. & Monaco, J.J. Intermediates in the formation of mouse 20S proteasomes: implications for the assembly of precursor beta subunits. EMBO J. 16, 5363-5375 (1997).
11. Ramos, P.C., Hockendorff, J., Johnson, E.S., Varshavsky, A. & Dohmen, R.J. Ump1p is required for proper maturation of the 20S proteasome and becomes its substrate upon completion of the assembly. Cell 92, 489-499 (1998).
12. Hirano, Y. et al. Cooperation of multiple chaperones required for the assembly of mammalian 20S proteasomes. Mol. Cell 24, 977-984 (2006).
13. Li, X., Kusmierczyk, A.R., Wong, P., Emili, A. & Hochstrasser, M. β-Subunit appendages promote 20S proteasome assembly by overcoming an Ump1-dependent checkpoint. EMBO J. 26, 2339-2349 (2007).
14. Yuan, X., Miller, M. & Belote, J.M. Duplicated proteasome subunit genes in Drosophila melanogaster encoding testes-specific isoforms. Genetics 144, 147-157 (1996).
15. De, M. et al. Beta2 subunit propeptides influence cooperative proteasome assembly. J. Biol. Chem. 278, 6153-6159 (2003).
16. Velichutina, I., Connerly, P.L., Arendt, C.S., Li, X. & Hochstrasser, M. Plasticity in eucaryotic 20S proteasome ring assembly revealed by a subunit deletion in yeast. EMBO J. 23, 500-510 (2004).
17. Enyenihi, A.H. & Saunders, W.S. Large-scale functional genomic analysis of sporulation and meiosis in Saccharomyces cerevisiae. Genetics 163, 47-54 (2003).
18. Dohmen, R.J., Willers, I. & Marques, A.J. Biting the hand that feeds: Rpn4-dependent feedback regulation of proteasome function. Biochim. Biophys. Acta 1773, 1599-604 (2007).
19. Pan, X. et al. A DNA integrity network in the yeast Saccharomyces cerevisiae. Cell 124, 1069-1081 (2006).
20. Chen, P. & Hochstrasser, M. Biogenesis, structure, and function of the yeast 20S proteasome. EMBO J. 14, 2620-2630 (1995).
21. Varshavsky, A. Regulated protein degradation. Trends Biochem. Sci. 30, 283-286 (2005).
22. Ravid, T., Kreft, S.G. & Hochstrasser, M. Membrane and soluble substrates of the Doa10 ubiquitin ligase are degraded by distinct pathways. EMBO J. 25, 533-543 (2006).
23. Krogan, N.J. et al. Global landscape of protein complexes in the yeast Saccharomyces cerevisiae. Nature 440, 637-643 (2006).
24. Isono, E. et al. The assembly pathway of the 19S regulatory particle of the yeast 26S proteasome. Mol. Biol. Cell 18, 569-580 (2006).
25. Schmidt, M. et al. The HEAT repeat protein Blm10 regulates the yeast proteasome by capping the core particle. Nat. Struct. Mol. Biol. 12, 294-303 (2005).
26. Altschul, S.F. et al. Gapped BLAST and PSI-BLAST: a new generation of protein database search programs. Nucleic Acids Res. 25, 3389-3402 (1997).
27. Le Tallec, B. et al. 20S Proteasome assembly is orchestrated by two distinct pairs of chaperones in yeast and in mammals. Mol. Cell 27, 660-674 (2007).
28. Groll, M. et al. A gated channel into the proteasome core particle. Nat. Struct. Biol. 7, 1062-1067 (2000).
29. Brennan, R.J. & Schiestl, R.H. Cadmium is an inducer of oxidative stress in yeast. Mutat. Res. 356, 171-178 (1996).
30. Inai, Y. & Nishikimi, M. Increased degradation of oxidized proteins in yeast defective in 26 S proteasome assembly. Arch. Biochem. Biophys. 404, 279-284 (2002).
31. Lee, S.C. & Shaw, B.D. A novel interaction between N-myristoylation and the 26S proteasome during cell morphogenesis. Mol. Microbiol. 63, 1039-1053 (2007).
32. Rivett, A.J., Bose, S., Brooks, P. & Broadfoot, K.I. Regulation of proteasome complexes by γ-interferon and phosphorylation. Biochimie 83, 363-366 (2001).
33. Liu, C.W., Corboy, M.J., DeMartino, G.N. & Thomas, P.J. Endoproteolytic activity of the proteasome. Science 299, 408-411 (2003).
34. Guthrie, C. & Fink, G.R. Guide to Yeast Genetics and Molecular Biology (Academic Press, San Diego, 1991).
35. 2+ reverse staining method for the detection and quantification of proteins in polyacrylamide gels. Anal. Biochem. 213, 206-212 (1993).
36. Verma, R. et al. Proteasomal proteomics: identification of nucleotide-sensitive proteasome-interacting proteins by mass spectrometric analysis of affinity-purified proteasomes. Mol. Biol. Cell 11, 3425-3439 (2000).
37. Elsasser, S., Schmidt, M. & Finley, D. Characterization of the proteasome using native gel electrophoresis. Methods Enzymol. 398, 353-363 (2005).