H2B ubiquitylation: The end is in sight

Biochimica et Biophysica Acta - Gene Structure and Expression

Volumn 1677, Issue 1-3, 2004, Pages 74-78

  Osley, Mary Ann ^a  

^a UNIVERSITY OF NEW MEXICO HEALTH SCIENCES CENTER   (United States)

Author keywords

Histone H2B ubiquitylation; Histone H3 methylation; Rad6

Indexed keywords

CHROMOSOME PROTEIN; HISTONE; PROTEIN; PROTEIN A24; PROTEIN H2B; UBIQUITIN; UNCLASSIFIED DRUG;

BUDDING; CHROMATIN; CHROMATIN STRUCTURE; CONJUGATION; DYNAMICS; EUKARYOTE; FUNGAL GENE; GENE DELETION; GENE EXPRESSION REGULATION; GENE MUTATION; GENE SILENCING; GENETIC ANALYSIS; GENETIC TRANSCRIPTION; HELA CELL; HUMAN; METHYLATION; NONHUMAN; PHENOTYPE; PRIORITY JOURNAL; PROTEIN ANALYSIS; PROTEIN DEGRADATION; PROTEIN DOMAIN; PROTEIN FUNCTION; PROTEIN ISOLATION; PROTEIN LOCALIZATION; PROTEIN METABOLISM; PROTEIN MODIFICATION; PROTEIN PHOSPHORYLATION; REGULATORY MECHANISM; REVIEW; SACCHAROMYCES CEREVISIAE; STOICHIOMETRY; STRUCTURE ANALYSIS; TELOMERE; UBIQUITINATION; YEAST;

ANIMALS; HISTONES; HUMANS; METHYLATION; SACCHAROMYCES CEREVISIAE; SACCHAROMYCES CEREVISIAE PROTEINS; TRANSCRIPTION, GENETIC; UBIQUITIN; UBIQUITIN-CONJUGATING ENZYMES;

EUKARYOTA; SACCHAROMYCETALES;

EID: 1542298300     PISSN: 01674781     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbaexp.2003.10.013     Document Type: Review

References (58)

1. Robzyk K., Recht J., Osley M.A. Rad6-dependent ubiquitination of histone H2B in yeast. Science. 287:2000;501-504.
2. Thorne A.W.et al. The structure of ubiquitinated histone H2B. EMBO J. 6:1987;1005-1010.
3. Luger K.et al. Crystal structure of the nucleosome core particle at 2.8 A resolution. Nature. 389:1997;251-260.
4. White C.L., Suto R.K., Luger K. Structure of the yeast nucleosome core particle reveals fundamental changes in internucleosome interactions. EMBO J. 20:2001;5207-5218.
5. Pickart C.M. Mechanisms underlying ubiquitination. Ann. Rev. Biochem. 70:2001;503-533.
6. Varshavsky A. The ubiquitin system. Trends Biochem. Sci. 22:1997;383-387.
7. Hershko A., Ciechanover A. The ubiquitin system. Ann. Rev. Biochem. 67:1998;425-479.
8. Hoege C.et al. RAD6-dependent DNA repair is linked to modification of PCNA by ubiquitin and SUMO. Nature. 419:2002;135-141.
9. Wood A.et al. Bre1, an E3 ubiquitin ligase required for recruitment and substrate selection of Rad6 at a promoter. Mol. Cell. 11:2003;267-274.
10. Hwang W.W.et al. A conserved RING finger protein required for histone H2B monoubiquitination and cell size control. Mol. Cell. 11:2003;261-266.
11. Bartel B., Wunning I., Varshavsky A. The recognition component of the N-end rule pathway. EMBO J. 9:1990;3179-3189.
12. Johnson R.E.et al. Saccharomyces cerevisiae RAD5-encoded DNA repair protein contains DNA helicase and zinc-binding sequence motifs and affects the stability of simple repetitive sequences in the genome. Mol. Cell. Biol. 12:1992;3807-3818.
13. Bailly V.et al. Yeast DNA repair proteins Rad6 and Rad18 form a heterodimer that has ubiquitin conjugating, DNA binding, and ATP hydrolytic activities. J. Biol. Chem. 272:1997;23360-23365.
14. Joazeiro C.A., Weissman A.M. RING finger proteins: mediators of ubiquitin ligase activity. Cell. 102:2000;549-552.
15. Krogan N.J.et al. RNA polymerase II elongation factors of Saccharomyces cerevisiae: a targeted proteomics approach. Mol. Cell. Biol. 22:2002;6979-6992.
16. Mueller C.L., Jaehning J.A. Ctr9, Rtf1, and Leo1 are components of the Paf1/RNA polymerase II complex. Mol. Cell. Biol. 22:2002;1971-1980.
17. Ng H.H., Dole S., Struhl K. The Rtf1 component of the Paf1 transcriptional elongation complex is required for ubiquitination of H2B. J. Biol. Chem. 278:2003;33625-33628.
18. Wood A.et al. The Paf1 complex is essential for histone monoubiquitination by the Rad6/Bre1 complex, which signals for histone methylation by COMPASS and Dot1p. J. Biol. Chem. 278:2003;34739-34742.
19. Bradbury E.M. Reversible histone modifications and the chromosome cell cycle. BioEssays. 14:1992;9-16.
20. Seale R.L. Rapid turnover of the histone-ubiquitin conjugate, protein A24. Nucleic Acids Res. 9:1981;3151-3158.
21. Wu R.S., Kohn K.W., Bonner W.M. Metabolism of ubiquitinated histones. J. Biol. Chem. 256:1981;5916-5920.
22. Goldknopf I.L.et al. Timing of ubiquitin synthesis and conjugation into protein A24 during the HeLa cell cycle. Biochem. Biophys. Res. Commun. 95:1980;1253-1260.
23. Amerik A.Y., Li S.J., Hochstrasser M. Analysis of the deubiquitinating enzymes of the yeast Saccharomyces cerevisiae. Biol. Chem. 381:2000;981-992.
24. Henry K.et al. Transcriptional activation via sequential histone H2B ubiquitylation and deubiquitylation, mediated by SAGA-associated Ubp8. Genes Dev. 17:2003;2648-2663.
25. Cheung P.et al. Synergistic coupling of histone H3 phosphorylation and acetylation in response to epidermal growth factor stimulation. Mol. Cell. 5:2000;905-915.
26. Lo W.S.et al. Phosphorylation of serine 10 in histone H3 is functionally linked in vitro and in vivo to Gcn5-mediated acetylation at lysine 14. Mol. Cell. 5:2000;917-926.
27. Lo W.S.et al. Snf1-a histone kinase that works in concert with the histone acetyltransferase Gcn5 to regulate transcription. Science. 293:2001;1142-1146.
28. Li J.et al. Involvement of histone methylation and phosphorylation in regulation of transcription by thyroid hormone receptor. Mol. Cell. Biol. 22:2002;5688-5697.
29. Rea S.et al. Regulation of chromatin structure by site-specific histone H3 methyltransferases. Nature. 406:2000;593-599.
30. Briggs S.D.et al. Gene silencing: trans-histone regulatory pathway in chromatin. Nature. 418:2002;498.
31. Bannister A.J., Schneider R., Kouzarides T. Histone methylation: dynamic or static? Cell. 109:2002;801-806.
32. Dover J.et al. Methylation of histone H3 by COMPASS requires ubiquitination of histone H2B by Rad6. J. Biol. Chem. 277:2002;28368-28371.
33. Briggs S.D.et al. Histone H3 lysine 4 methylation is mediated by Set1 and required for cell growth and rDNA silencing in Saccharomyces cerevisiae. Genes Dev. 15:2001;3286-3295.
34. Bryk M.et al. Evidence that Set1, a factor required for methylation of histone H3, regulates rDNA silencing in S. cerevisiae by a Sir2-independent mechanism. Curr. Biol. 12:2002;165-170.
35. Feng Q.et al. Methylation of H3-lysine 79 is mediated by a new family of HMTases without a SET domain. Curr. Biol. 12:2002;1052-1058.
36. van Leeuwen F., Gafken P.R., Gottschling D.E. Dot1p modulates silencing in yeast by methylation of the nucleosome core. Cell. 109:2002;745-756.
37. Sun Z.W., Allis C.D. Ubiquitination of histone H2B regulates H3 methylation and gene silencing in yeast. Nature. 418:2002;104-108.
38. Ng H.H.et al. Ubiquitination of histone H2B by Rad6 is required for efficient Dot1-mediated methylation of histone H3 lysine 79. J. Biol. Chem. 277:2002;34655-34657.
39. Jason L.J.et al. Histone ubiquitination: a tagging tail unfolds? BioEssays. 24:2002;166-174.
40. Davies N., Lindsey G.G. Histone H2B (and H2A) ubiquitination allows normal histone octamer and core particle reconstitution. Biochim. Biophys. Acta. 1218:1994;187-193.
41. Henry K.W., Berger S.L. Trans-tail histone modifications: wedge or bridge? Nat. Struct. Biol. 9:2002;565-566.
42. Buchberger A. From UBA to UBX: new words in the ubiquitin vocabulary. Trends Cell Biol. 12:2002;216-221.
43. Prag G.et al. Mechanism of ubiquitin recognition by the CUE domain of Vps9p. Cell. 113:2003;609-620.
44. Kang R.S.et al. Solution structure of a CUE-ubiquitin complex reveals a conserved mode of ubiquitin binding. Cell. 113:2003;621-630.
45. Krogan N.J.et al. The Paf1 complex is required for histone H3 methylation by COMPASS and Dot1p: linking transcriptional elongation to histone methylation. Mol. Cell. 11:2003;721-729.
46. Barsoum J., Varshavsky A. Preferential localization of variant nucleosomes near the 5′-end of the mouse dihydrofolate reductase gene. J. Biol. Chem. 260:1985;7688-7697.
47. Davie J.R., Murphy L.C. Level of ubiquitinated histone H2B in chromatin is coupled to ongoing transcription. Biochemistry. 29:1990;4752-4757.
48. Davie J.R., Lin R., Allis C.D. Timing of the appearance of ubiquitinated histones in developing new macronuclei of Tetrahymena thermophila. Biochem. Cell. Biol. 69:1991;66-71.
49. Hensold J.O., Swerdlow P.S., Housman D.E. A transient increase in histone H2A ubiquitination is coincident with the onset of erythroleukemic cell differentiation. Blood. 71(4):1988;1153-1156.
50. Levinger L., Varshavsky A. Selective arrangement of ubiquitinated and D1 protein-containing nucleosomes within the Drosophila genome. Cell. 28:1982;375-385.
51. Nickel B.E., Allis C.D., Davie J.R. Ubiquitinated histone H2B is preferentially located in transcriptionally active chromatin. Biochemistry. 28:1989;958-963.
52. Turner S.D.et al. The E2 ubiquitin conjugate Rad6 is required for the ArgR/Mcm1 repression of ARG1 transcription. Mol. Cell. Biol. 22:2002;4011-4019.
53. Huang H.et al. The ubiquitin-conjugating enzyme Rad6 (Ubc2) is required for silencing in Saccharomyces cerevisiae. Mol. Cell. Biol. 17:1997;6693-6699.
54. Bernstein B.E.et al. Methylation of histone H3 Lys 4 in coding regions of active genes. Proc. Natl. Acad. Sci. U. S. A. 99:2002;8695-8700.
55. Santos-Rosa H.et al. Active genes are tri-methylated at K4 of histone H3. Nature. 419:2002;407-411.
56. Ng H.H.et al. Lysine-79 of histone H3 is hypomethylated at silenced loci in yeast and mammalian cells: a potential mechanism for position-effect variegation. Proc. Natl. Acad. Sci. U. S. A. 100:2003;1820-1825.
57. Ng H.H.et al. Targeted recruitment of Set1 histone methylase by elongating Pol II provides a localized mark and memory of recent transcriptional activity. Mol. Cell. 11:2003;709-719.
58. van Leeuwen F., Gottschling D.E. Genome-wide histone modifications: gaining specificity by preventing promiscuity. Curr. Opin. Cell Biol. 14:2002;756-762.