Cellular memory and the histone code

Cell

Volumn 111, Issue 3, 2002, Pages 285-291

  Turner, Bryan M ^a  

^a UNIVERSITY DEPARTMENT OF MEDICINE   (United Kingdom)

Author keywords

[No Author keywords available]

Indexed keywords

ENZYME; HISTONE; HISTONE DEACETYLASE; HISTONE H3; HISTONE H4; METHYLTRANSFERASE;

ACETYLATION; AMINO ACID SUBSTITUTION; CATALYSIS; CELL FUNCTION; CHROMATIN CONDENSATION; CHROMATIN STRUCTURE; COMBINATORIAL CHEMISTRY; GENE EXPRESSION; GENETIC TRANSCRIPTION; GENOME; HETEROCHROMATIN; HUMAN; NONHUMAN; NUCLEOSOME; PRIORITY JOURNAL; PROTEIN FUNCTION; PROTEIN METHYLATION; PROTEIN MODIFICATION; PROTEIN PROTEIN INTERACTION; REVIEW; SURFACE PROPERTY; TRANSCRIPTION INITIATION;

EID: 0036850325     PISSN: 00928674     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0092-8674(02)01080-2     Document Type: Review

References (38)

1. Agalioti T., Chen G., Thanos D. Deciphering the transcriptional histone acetylation code for a human gene. Cell. 111:2002;381-392. this issue,
2. Beisel C., Imhof A., Greene J., Kremmer E., Sauer F. Histone methylation by the Drosophila epigenetic regulator Ash1. Nature. 419:2002;857-862. Published online October 9, 2002. 10.1038/nature01126.
3. Bernstein B.E., Humphrey E.L., Erlich R.L., Schneider R., Bouman P., Liu J.S., Kouzarides T., Schreiber S.L. Methylation of histone H3 Lys 4 in coding regions of active genes. Proc. Natl. Acad. Sci. USA. 99:2002;8695-8700.
4. Bird A. DNA methylation patterns and epigenetic memory. Genes Dev. 16:2002;6-21.
5. Briggs S.D., Xiao T., Sun Z.W., Caldwell J.A., Shabanowitz J., Hunt D.F., Allis C.D., Strahl B.D. Gene silencing. trans-histone gene regulatory pathway in chromatin Nature. 418:2002;498.
6. Bryk M., Briggs S.D., Strahl B.D., Curcio M.J., Allis C.D., Winston F. 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.
7. Czermin B., Schotta G., Hulsmann B.B., Brehm A., Becker P.B., Reuter G., Imhof A. Physical and functional association of SU(VAR)3-9 and HDAC1 in Drosophila. EMBO Rep. 2:2001;915-919.
8. Czermin B., Melfi R., McCabe D., Seitz V., Imhof A., Pirrotta V. Drosophila Enhancer of Zeste/ESC complexes have a histone H3 methyltransferase activity that marks chromosomal Polycomb sites. Cell. 111:2002;185-196.
9. Daujat S., Bauer U.-M., Shah V., Turner B.M., Berger S., Kouzarides T. Cross-talk between CARM1 methylation and CBP acetylation on histone H3. Curr. Biol. in press:2002.
10. Dover J., Schneider J., Boateng M.A., Wood A., Dean K., Johnston M., Shilatifard A. Methylation of histone H3 by COMPASS requires ubiquitination of histone H2B by Rad6. J. Biol. Chem. 277:2002;28368-28371.
11. Fang J., Feng Q., Ketel C.S., Wang H., Cao R., Xia L., Erdjument-Bromage H., Tempst P., Simon J.A., Zhang Y. Purification and functional characterization of SET8, a nucleosomal histone H4-lysine 20-specific methyltransferase. Curr. Biol. 12:2002;1086-1099.
12. Feng Q., Wang H., Ng H.H., Erdjument-Bromage H., Tempst P., Struhl K., Zhang Y. Methylation of H3-lysine 79 is mediated by a new family of HMTases without a SET domain. Curr. Biol. 12:2002;1052-1058.
13. Hassan A.H., Prochasson P., Neely K.E., Galasinski S.C., Chandy M., Carrozza M.J., Workman J.L. Function and selectivity of bromodomains in anchoring chromatin-modifying complexes to promoter nucleosomes. Cell. 111:2002;369-379. this issue,
14. Jacobs S.A., Khorasanizadeh S. Structure of HP1 chromodomain bound to a lysine 9-methylated histone H3 tail. Science. 295:2002;2080-2083.
15. Jenuwein T., Allis C.D. Translating the histone code. Science. 293:2001;1074-1080.
16. Luger K., Mader A.W., Richmond R.K., Sargent D.F., Richmond T.J. Crystal structure of the nucleosome core particle at 2.8Å resolution. Nature. 389:1997;251-260.
17. Müller J., Hart C.M., Francis N.J., Vargas M.L., Sengupta A., Wild B., Miller E.L., O'Connor M.B., Kingston R.E., Simon J.A. Histone methyltransferase activity of a Drosophila Polycomb Group repressor complex. Cell. 111:2002;197-208.
18. Nakayama J., Rice J.C., Strahl B.D., Allis C.D., Grewal S.I.S. Role of histone H3 lysine 9 methylation in epigenetic control of heterochromatin assembly. Science. 292:2001;110-113.
19. Ng H.H., Feng Q., Wang H., Erdjument-Bromage H., Tempst P., Zhang Y., Struhl K. Lysine methylation within the globular domain of histone H3 by Dot1 is important for telomeric silencing and Sir protein association. Genes Dev. 16:2002;1518-1527.
20. Nielsen P.R., Nietlispach D., Mott H.R., Callaghan J., Bannister A., Kouzarides T., Murzin A.G., Murzina M.V., Laue E.D. Structure of the HP1 chromodomain bound to histone H3 methylated at lysine 9. Nature. 416:2002;103-107.
21. Nishioka K., Chuikov S., Sarma K., Erdjument-Bromage H., Allis C.D., Tempst P., Reinberg D. Set9, a novel histone H3 methyltransferase that facilitates transcription by precluding histone tail modifications required for heterochromatin formation. Genes Dev. 16:2002;479-489. a.
22. Nishioka K., Rice J.D., Sarma K., Erdjument-Broamge H., Werner J., Wang Y., Chuikov S., Valenzuela P., Tempst P., Steward R.et al. PR-Set7 is a nucleosome-specific methyltransferase that modifies lysine 20 of histone H4 and is associated with silent chromatin. Mol. Cell. 9:2002;1201-1213. b.
23. Rea S., Eisenhaber F., O'Carroll D., Strahl B.D., Sun Z.-W., Schmid M., Opravil S., Mechtler K., Ponting C.P., Allis C.D., Jenuwein T. Regulation of chromatin structure by site-specific histone H3 methyltransferases. Nature. 406:2000;593-599.
24. Rice J.D., Nishioka K., Sarma K., Steward R., Reinberg D., Allis C.D. Mitotic-specific methylation of histone H4 Lys 20 follows increased PR-Set7 expression and its localization to mitotic chromosomes. Genes Dev. 16:2002;2225-2230.
25. Richards E.J., Elgin S.C.R. Epigenetic codes for heterochromatin formation and silencing. rounding up the usual suspects Cell. 108:2002;489-500.
26. Santos-Rosa H., Schneider R., Bannister A.J., Sherriff J., Bernstein B.E., Emre N.C., Schreiber S.L., Mellor J., Kouzarides T. Active genes are tri-methylated at K4 of histone H3. Nature. 419:2002;407-411.
27. Selker E.U., Freitag M., Kothe G.O., Margolin B.S., Rountree M.R., Allis C.D., Tamaru H. Induction and maintenance of nonsymmetrical DNA methylation in Neurospora. Proc. Natl. Acad. Sci. USA. in press. 2002;. Published online August 20, 2002. 10.1073/pnas.182427299.
28. Spotswood H.T., Turner B.M. An increasingly complex code. J. Clin. Invest. 110:2002;577-582.
29. Sun Z.-W., Allis C.D. Ubiquitination of histone H2B regulates H3 methylation and gene silencing in yeast. Nature. 418:2002;104-108.
30. Tachibana M., Sugimoto K., Fukushima T., Shinkai Y. Set domain-containing protein, G9a, is a novel lysine-preferring mammalian histone methyltransferase with hyperactivity and specific selectivity to lysines 9 and 27 of histone H3. J. Biol. Chem. 276:2001;25309-25317.
31. Turner B.M. Decoding the nucleosome. Cell. 75:1993;5-8.
32. 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.
33. Vandel L., Trouche D. Physical association between the histone acetyl transferase CBP and a histone methyl transferase. EMBO Rep. 2:2000;21-26.
34. Volpe T.A., Kidner C., Hall I.M., Teng G., Grewal S.I.S., Martienssen R.A. Regulation of heterochromatic silencing and histone H3 lysine-9 methylation by RNAi. Science. 297:2002;1833-1837.
35. Wang H., Cao R., Xia L., Erdjument-Bromage H., Borchers C., Tempst P., Zhang Y. Purification and functional characterization of a histone H3-lysine 4-specific methyltransferase. Mol. Cell. 8:2001;1207-1217.
36. Zegerman P., Canas B., Pappin D., Kouzarides T. Histone H3 lysine 4 methylation disrupts binding of nucleosome remodelling and deacetylase (NuRD) repressor complex. J. Biol. Chem. 277:2002;11621-11624.
37. Zeng L., Zhou M.M. Bromodomain. an acetyl-lysine binding domain FEBS Lett. 513:2002;124-128.
38. Zhang Y., Reinberg D. Transcription regulation by histone methylation. interplay between different covalent modifications of the core histone tails Genes Dev. 15:2001;2343-2360.