The proteasome: A utility tool for transcription?

Current Opinion in Genetics and Development

Volumn 16, Issue 2, 2006, Pages 197-202

  Collins, Galen A ^a   Tansey, William P ^a  

^a Watson School of Biological Sciences   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

ADENOSINE TRIPHOSPHATASE; CELL CYCLE PROTEIN 20; PROTEASOME; RNA POLYMERASE; TRANSCRIPTION FACTOR;

BIOLOGICAL ACTIVITY; CHROMATIN; GENE CONTROL; GENETIC TRANSCRIPTION; PRIORITY JOURNAL; PROTEIN DEGRADATION; PROTEIN STRUCTURE; REVIEW;

ANIMALS; HUMANS; MODELS, BIOLOGICAL; MODELS, CHEMICAL; PROTEASOME ENDOPEPTIDASE COMPLEX; TRANSCRIPTION, GENETIC;

EID: 33644867538     PISSN: 0959437X     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.gde.2006.02.009     Document Type: Review

References (47)

1. J.C. Swaffield, J.F. Bromberg, and S.A. Johnston Alterations in a yeast protein resembling HIV Tat-binding protein relieve requirement for an acidic activation domain in Gal4 Nature 357 1992 698 700
2. D.M. Rubin, O. Coux, I. Wefes, C. Hengartner, R.A. Young, A.L. Goldberg, and D. Finley Identification of the gal4 suppressor Sug1 as a subunit of the yeast 26S proteasome Nature 379 1996 655 657
3. R. St-Arnaud Dual functions for transcriptional regulators: myth or reality? J Cell Biochem (Supplement) 32/33 1999 32 40
4. J.R. Lipford, and R.J. Deshaies Diverse roles for ubiquitin-dependent proteolysis in transcriptional activation Nat Cell Biol 5 2003 845 850
5. M. Muratani, and W.P. Tansey How the ubiquitin-proteasome system controls transcription Nat Rev Mol Cell Biol 4 2003 192 201
6. M.H. Glickman, and A. Ciechanover The ubiquitin-proteasome proteolytic pathway: destruction for the sake of construction Physiol Rev 82 2002 373 428
7. N. Benaroudj, P. Zwickl, E. Seemüller, W. Baumeister, and A.L. Goldberg ATP hydrolysis by the proteasome regulatory complex PAN serves multiple functions in protein degradation Mol Cell 11 2003 69 78
8. S. Elsasser, D. Chandler-Militello, B. Müller, J. Hanna, and D. Finley Rad23 and Rpn10 serve as alternative ubiquitin receptors for the proteasome J Biol Chem 279 2004 26817 26822
9. R. Verma, R. Oania, J. Graumann, and R.J. Deshaies Multiubiquitin chain receptors define a layer of substrate selectivity in the ubiquitin-proteasome system Cell 118 2004 99 110
10. A. Guterman, and M.H. Glickman Complementary roles for Rpn11 and Ubp6 in deubiquitination and proteolysis by the proteasome J Biol Chem 279 2004 1729 1738
11. R. Verma, L. Aravind, R. Oania, W.H. McDonald, J.R. Yates, E.V. Koonin, and R.J. Deshaies Role of Rpn11 metalloprotease in deubiquitination and degradation by the 26S proteasome Science 298 2002 611 615
12. C.-W. Liu, M.J. Corboy, G.N. DeMartino, and P.J. Thomas Endoproteolytic activity of the proteasome Science 299 2003 408 411
13. F. Gonzalez, A. Delahodde, T. Kodadek, and S.A. Johnston Recruitment of a 19S proteasome subcomplex to an activated promoter Science 296 2002 548 550
14. L. Sun, S.A. Johnston, and T. Kodadek Physical association of the APIS complex and general transcription factors Biochem Biophys Res Commun 296 2002 991 999
15. M.C. Morris, P. Kaiser, S. Rudyak, C. Baskerville, M.H. Watson, and S.I. Reed Cks1-dependent proteasome recruitment and activation of CDC20 transcription in budding yeast Nature 423 2003 1009 1013
16. T.G. Gillette, F. Gonzalez, A. Delahodde, S.A. Johnston, and T. Kodadek Physical and functional association of RNA polymerase II and the proteasome Proc Natl Acad Sci USA 101 2004 5904 5909 The authors demonstrate that proteasome inhibitors impair the recognition of termination sites. The authors also show that the 20S complex is enriched at the 3′ ends of genes.
17. S.E. Babbitt, A. Kiss, A.E. Deffenbaugh, Y.-H. Chang, E. Bailly, H. Erdjument-Bromage, P. Tempst, T. Buranda, L.A. Sklar, and J. Baumler ATP Hydrolysis-Dependent Disassembly of the 26S Proteasome Is Part of the Catalytic Cycle Cell 121 2005 553 565 The authors show that the 19S components can disassociate from the 20S sub-complex after proteolysis of substrates. This has important ramifications for mechanisms of proteolysis and supports a possible function of the 19S base that is independent of other 26S subunits.
18. N.J. Krogan, M.H.Y. Lam, J. Filingham, M.-C. Keogh, M. Gebbia, J. Li, N. Datta, G. Cagney, S. Buratowski, and A. Emili Proteasome involvement in the repair of DNA double-strand breaks Mol Cell 16 2004 1027 1034
19. D. Smith, G. Kafri, Y. Cheng, D. Ng, T. Walz, and A. Goldberg ATP binding to PAN or the 26S ATPases causes association with the 20S proteasome, gate opening, and translocation of unfolded proteins Mol Cell 9 2005 687 698 The authors use the archaeal PAN complex to study the association of a 19S base with the 20S sub-complex. They show that this process requires the binding of ATP but not its hydrolysis. This supports the idea that the archaeal PAN complex and possibly the 19S regulatory complex function independently and associate transiently with the 20S sub-complex.
20. E. Ezhkova, and W.P. Tansey Proteasomal ATPases link ubiquitylation of histone H2B to methylation of histone H3 Mol Cell 13 2004 435 442 This study reveals proteasome ATPases at promoter sequences before activation signals. Following activation, the proteasome is found across the gene. This study further shows that proteasome ATPases are recruited to chromatin in an H2B ubiquitin-dependent process, and that proteasome ATPases are necessary for H3 methylation at lysine residues 4 and 79.
21. V.P.C.C. Yu, C. Baskerville, B. Grunenfelder, and S.I. Reed A kinase-independent function of Cks1 and Cdk1 in regulation of transcription Mol Cell 17 2005 145 151
22. E. Chiari, I. Lamsoul, J. Lodewick, C. Chopin, F. Bex, and C. Pique Stable ubiquitination of human T-cell leukemia virus type 1 Tax is required for proteasome binding J Virol 78 2004 11823 11832 The authors show that ubiquitylation of the viral transcription activator Tax is necessary for the efficient association of Tax with the proteasome.
23. F.E. Kleiman, F. Wu-Baer, D. Fonseca, S. Kaneko, R. Baer, and J.L. Manley BRCA1/BARD1 inhibition of mRNA 3′ processing involves targeted degradation of RNA polymerase II Genes Dev 19 2005 1227 1237
24. J. Reid, and J.Q. Svejstrup DNA damage-induced Def1-RNA polymerase II interaction and Def1 requirement for polymerase ubiquitylation in vitro J Biol Chem 279 2004 29875 29878
25. B.P. Somesh, J. Reid, W.-F. Liu, T.M.M. Søgaard, H. Erdjument-Bromage, P. Tempst, and J.Q. Svejstrup Multiple mechanisms confining RNA polymerase II ubiquitylation to polymerases undergoing transcriptional arrest Cell 121 2005 913 923
26. C.J. Fryer, J.B. White, and K.A. Jones Mastermind recruits CycC:CDK8 to phosphorylate the notch ICD and coordinate activation with turnover Mol Cell 16 2004 509 520
27. S.Y. Kim, A. Herbst, K.A. Tworkowski, S.E. Salghetti, and W.P. Tansey Skp2 regulates Myc protein stability and activity Mol Cell 11 2003 1177 1188
28. M. Muratani, C. Kung, K.M. Shokat, and W.P. Tansey The F box protein Dsg1/Mdm30 is a transcriptional coactivator that stimulates Gal4 turnover and cotranscriptional mRNA processing Cell 120 2005 887 899 This study shows that defects in the ubiquitylation and stability of the transcription activator Gal4 are associated with proper phosphorylation of RNA pol II and pre-mRNA processing.
29. G. Reid, M.R. Hubner, R. Metivier, H. Brand, S. Denger, D. Manu, J. Beaudouin, J. Ellenberg, and F. Gannon Cyclic, proteasome-mediated turnover of unliganded and liganded ERα on responsive promoters is an integral feature of estrogen signaling Mol Cell 11 2003 695 707
30. S.E. Salghetti, M. Muratani, H. Wijnen, B. Futcher, and W.P. Tansey Functional overlap of sequences that activate transcription and signal ubiquitin-mediated proteolysis Proc Natl Acad Sci USA 97 2000 3118 3123
31. N. von der Lehr, S. Johansson, S. Wu, F. Bahram, A. Castell, C. Cetinkaya, P. Hydbring, I. Weidung, K. Nakayama, and K.I. Nakayama The F-box protein Skp2 participates in c-Myc proteosomal degradation and acts as a cofactor for c-Myc-regulated transcription Mol Cell 11 2003 1189 1200
32. W.P. Tansey Transcriptional activation: risky business Genes Dev 15 2001 1045 1050
33. A.P. Dennis, D.M. Lonard, Z. Nawaz, and B.W. O'Malley Inhibition of the 26S proteasome blocks progesterone receptor-dependent transcription through failed recruitment of RNA polymerase II J Steroid Biochem Mol Biol 94 2005 337 346 The authors show that proteasome inhibitors prevent progesterone receptor-dependent transcription by interfering with pol II recruitment to promoters. The authors go on to show that re-initiation of transcription requires the proteolytic function of the proteasome.
34. J.R. Lipford, G.T. Smith, Y. Chi, and R.J. Deshaies A putative stimulatory role for turnover in gene expression Nature 438 2005 113 116 The authors find that ubiquitylation of Gcn4, and the proteolytic function of the proteasome are necessary for transcription and the stable recruitment of RNA pol II at promoters. The fact that the ubiquitylation of Gcn4 depends on kinases associated with RNA pol II suggests that the proteolytic functions of the proteasome are crucial for re-initiation of transcription.
35. O.H. Kramer, P. Zhu, H.P. Ostendorff, M. Golebiewski, J. Tiefenbach, M.A. Peters, B. Brill, B. Groner, I. Bach, and T. Heinzel The histone deacetylase inhibitor valproic acid selectively induces proteasomal degradation of HDAC2 EMBO J 22 2003 3411 3420
36. R. Métivier, G. Penot, M.R. Hübner, G. Reid, H. Brand, M. Kos, and F. Gannon Estrogen receptor-α directs ordered, cyclical and combinatorial recruitment of cofactors on a natural target promoter Cell 115 2003 751 763
37. H.P. Ostendorff, R.I. Peirano, M.A. Peters, A. Schluter, M. Bossenz, M. Scheffner, and I. Bach Ubiquitination-dependent cofactor exchange on LIM homeodomain transcription factors Nature 416 2002 99 103
38. V. Perissi, A. Aggarwal, C.K. Glass, D.W. Rose, and M.G. Rosenfeld A corepressor/coactivator exchange complex required for transcriptional activation by nuclear receptors and other regulated transcription Factors Cell 116 2004 511 526 The authors show that the exchange of co-repressors with coactivators depends on the ubiquitin ligases TBL1 (transducin β-like protein 1) and TBLR1 (TBL-related protein 1). The authors go on to propose a model in which the 19S base regulates this exchange.
39. B.C. Braun, M. Glickman, R. Kraft, B. Dahlmann, P.-M. Kloetzel, D. Finley, and M. Schmidt The base of the proteasome regulatory particle exhibits chaperone-like activity Nat Cell Biol 1 1999 221 226
40. C.-w. Liu, L. Millen, T.B. Roman, H. Xiong, H.F. Gilbert, R. Noiva, G.N. DeMartino, and P.J. Thomas Conformational remodeling of proteasomal substrates by PA700, the 19S regulatory complex of the 26S proteasome J Biol Chem 277 2002 26815 26820
41. A. Navon, and A.L. Goldberg Proteins are unfolded on the surface of the ATPase ring before transport into the proteasome Mol Cell 8 2001 1339 1349
42. A. Ferdous, F. Gonzalez, L. Sun, T. Kodadek, and S.A. Johnston The 19S regulatory particle of the proteasome is required for efficient transcription elongation by RNA polymerase II Mol Cell 7 2001 981 991
43. D. Lee, E. Ezhkova, B. Li, S.G. Pattenden, W.P. Tansey, and J.L. Workman The proteasome regulatory particle alters the SAGA coactivator to enhance its interactions with transcription factors Cell 123 2005 423 436 This study reveals that the 19S sub-complex is important for recruitment of the transcriptional complex SAGA. The 19S sub-complex increases the affinity of SAGA for the activator Gal4, and SAGA's histone acetyltransferase activity. Mutations in the 19S base subunit Rpt6 impair binding of SAGA, TATA-binding protein (TBP), and RNA pol II at the GAL1 promoter.
44. B. Stillman Origin recognition and the chromosome cycle FEBS Lett 579 2005 877 884
45. L. Warfield, J.A. Ranish, and S. Hahn Positive and negative functions of the SAGA complex mediated through interaction of Spt8 with TBP and the N-terminal domain of TFIIA Genes Dev 18 2004 1022 1034
46. B.C. Freeman, and K.R. Yamamoto Disassembly of transcriptional regulatory complexes by molecular chaperones Science 296 2002 2232 2235
47. D.A. Stavreva, W.G. Muller, G.L. Hager, C.L. Smith, and J.G. McNally Rapid glucocorticoid receptor exchange at a promoter is coupled to transcription and regulated by chaperones and proteasomes Mol Cell Biol 24 2004 2682 2697 The authors show that glucocorticoid receptor exchange is a balance of the stabilizing effects of Hsp90 and the destabilizing effects of the proteasome. The authors go on to show that the dynamics of the glucocorticoid receptor on the promoter correlates with transcriptional activity.