Чарльз Эллис - Эпигенетика

Grant P.A., Eberharter A., John S., Cook R.G., Turner B.M., and Workman J.L., 1999. Expanded lysine acetylation specificity of Gcn5 in native complexes. J. Biol. Chem. 274: 5895-5900.

Hake S.B. and Allis C.D., 2006. Histone H3 variants and their potential role in indexing mammalian genomes: The “H3 barcode hypothesis”. Proc. Natl. Acad. Sci. 103: 6428-6435.

Hake S.B., Garcia B.A., Kauer M., Baker S.P., Shabanowitz J., Hunt D.F., and Allis C.D., 2005. Serine 31 phosphorylation of histone variant H3.3 is specific to regions bordering centromeres in metaphase chromosomes. Proc. Natl. Acad. Sci. 102: 6344-6349.

Hamamoto R., Furukawa Y., Morita M., Iimura Y., Silva F.P., Li M., Yagyu R., and Nakamura Y., 2004. SMYD3 encodes a histone methyltransferase involved in the proliferation of cancer cells. Nat. Cell Biol. 6: 731-740.

Harvey A.C., Jackson S.P., and Downs J.A., 2005. Saccharomyces cerevisiae histone H2A Seri22 facilitates DNA repair. Genetics 170:543-553.

Hayashi K., Yoshida K., and Matsui Y., 2005. A histone H3 methyltransferase controls epigenetic events required for meiotic prophase. Nature 438:374-378.

He Z., ChoY.Y., Ma W.Y., Choi H.S., Bode A.M., and DongZ., 2005. Regulation of ultraviolet B-induced phosphorylation of histone H3 at serine 10 by Fyn kinase. J. Biol. Chem. 280:2446-2454.

Hendzel M.J., Wei Y., Mancini M.A., Van Hooser A., Ranalli T., Brinkley B.R., Bazett-Jones D.P., and Allis C.D., 1997. Mitosis-specific phosphorylation of histone H3 initiates primarily within pericentromeric heterochromatin during G2 and spreads in an ordered fashion coincident with mitotic chromosome condensation. Chromosoma 106:348-360.

Hsu J.Y., Sun Z.W., Li X., Reuben M., Tatchell K., Bishop D.K., Grushcow J.M., Brame C.J., Caldwell J.A., Hunt D.E, et al., 2000. Mitotic phosphorylation of histone H3 is governed by Ipll/aurora kinase and Glc7/PPI phosphatase in budding yeast and nematodes. Cell 102:279-291.

Hyland E.M., Cosgrove M.S., Molina H., Wang D., Pandey A., Cot-tee R.J., and Boeke J.D., 2005. Insights into the role of histone H3 and histone H4 core modifiable residues in Saccharomyces cerevisiae. Mol. Cell. Biol. 25:10060-10070.

Ichijima Y., Sakasai R., Okita N., Asahina K., Mizutani S., and Te-raoka H., 2005. Phosphoiylation of histone H2AXat M phase in human cells without DNA damage response. Biochem. Biophys. Res. Commun. 336: 807-812.

Jackson J.P., Lindroth A.M., Cao X., and Jacobsen S.E., 2002. Control of CpNpG DNA methylation by the KRYPTON ITE histone H3 methyltransferase. Nature 416:556-560.

Jackson J.P., Johnson L., JasencakovaZ., ZhangX., PerezBurgos L., Singh P.B., Cheng X., Schubert I., Jenuwein T., and Jacobsen S.E., 2004. Dimethylation of histone H3 lysine 9 is a critical mark for DNA methylation and gene silencing in Arabidopsis thaliana. Chromsoma 112:308-315.

Jeppesen P. and Turner B.M., 1993. The inactive X chromosome in female mammals is distinguished by a lack of histone H4 acetylation, a cytogenetic marker for gene expression Cell 74:281-289.

Jin Y., Wang Y., Walker D.L., Dong H., Conley C., Johansen J., and Johansen K.M., 1999. JIL-1: A novel chromosomal tandem kinase implicated in transcriptional regulation in Drosophila. Mol. Cell 4: 129-135.

Kao C.F., Hillyer C., Tsukuda T., Henry K., Berger S., and Osley M. A., 2004. Rad6 plays a role in transcriptional activation through ubiquitylation of histone H2B. Genes Dev. 18:184-195.

Kapetanaki M.G., Guerrero-Santoro J., Bisi D.C., Hsieh C.L., Rapic-Otrin V., and Levine A.S., 2006. The DDB1-CUL4AD-DB2 ubiquitin ligase is deficient in xeroderma pigmentosum group E and targets histone H2A at UV-damaged DNA sites. Proc. Natl. Acad. Sci. 103:2588-2593.

Kawasaki H., Taira K., and Yokoyama K., 2000. Histone acetyltransferase (HAT) activity of ATF-2 is necessary for the CRE-dependent transcription. Nucleic Acids Symp. Ser., 2000:259-260.

Kawasaki H., Schiltz L., Chiu R., Itakura K., Taira K., Nakatani Y., and Yokoyama K.K., 2000. ATF-2 has intrinsic histone acetyltransferase activity which is modulated by phosphorylation. Nature 405:195-200.

Kim K.C., Geng L., and Huang S., 2003. Inactivation of a histone methyltransferase by mutations in human cancers. Cancer Res. 63:7619-7623.

Kimura A. and Horikoshi M., 1998. Tip60 acetylates six lysines of a specific class in core histones in vitro. Genes Cells 3:789-800.

KizerK.O., Phatnani H.P., ShibataY., Hall H., GreenleafAL., and Strahl B.D., 2005. A novel domain in Set2 mediates RNA polymerase II interaction and couples histone H3 K36 methylation with transcript elongation. Mol. Cell. Biol. 25:3305-3316.

Kleff S., Andrulis E.D., Anderson C.W., and Stemglanz R., 1995. Identification of a gene encoding a yeast histone H4 acetyltransferase. J. Biol. Chem. 270:24674-24677.

Kothapalli N., Sarath G., and Zempleni J., 2005a. Biotinylation of K12 in histone H4 decreases in response to DNA double-strand breaks in human JAr choriocarcinoma cells. J. Nutr. 135:2337-2342.

Kothapalli N., Camporeale G., Kueh A., Chew Y.C., Oommen A.M., Griffin J.B., and Zempleni J., 2005b. Biological functions of biotinylated histones. J. Nutr. Biochem. 16:446-448.

Kruhlak M.J., Hendzel M.J., Fischle W., Bertos N.R., Hameed S., Yang X.J., Verdin E., and Bazett-Jones D.P., 2001. Regulation of global acetylation in mitosis through loss of histone acetyl-transferases and deacetylases from chromatin. J. Biol Chem. 276:38307-38319.

Kuo M.H., Brownell I.E., Sobel R.E., RanalliT.A., Cook R.G., Edmondson D.G., Roth S.Y., and Allis C.D., 1996. Transcription-linked acetylation by Gcn5p of histones H3 and H4 at specific lysines Nature 383:269-272.

Kuzmichev A., Jenuwein T., Tempst P., and Reinberg D., 2004. Different EZH2-containing complexes target methylation of histone HI or nucleosomal histone H3. Mol. Cell 14:183-193.

Kuzmichev A., Nishioka K., Erdjument-Bromage H., Tempst P., and Reinberg D., 2002. Histone methyltransferase activity associated with a human multiprotein complex containing the Enhancer of Zeste protein. Genes Dev. 16:2893-2905.

Lachner M., O’Carroll D., Rea S., Mechtler K., and Jenuwein T., 2001 Methylation of histone H3 lysine 9 creates a binding site for HP1 proteins. Nature 410:116-120.

Lacoste N., Utley R.T., Hunter J.M., Poirier G.G., and Cote J., 2002. Disrupter of telomeric silencing-1 is a chromatin-specific histone H3 methyltransferase./. Biol. Chem. 277: 30421-30424.

Lo W.S., Duggan L., Emre N.C, Belotserkovskya R., Lane W.S., Shiekhattar R., and Berger S.L., 2001. Snfl — A histone kinase that works in concert with the histone acetyltransferase Gcn5 to regulate transcription. Science 293:1142-1146.

Maile T., Kwoczynski S., Katzenberger R.J., Wassarman D.A., and Sauer F., 2004. TAF1 activates transcription by phosphorylation of serine 33 in histone H2B. Science 304:1010-1014.

McKittrick E., Gafken P.R., Ahmad K., and HenikoffS., 2004. Histone H3.3 is enriched in covalent modifications associated with active chromatin. Proc. Natl. Acad. Sci. 101:1525-1530.

Milne T.A., Briggs S.D., Brock H.W., Martin M.E., Gibbs D., Allis C.D., and Hess J.L., 2002. MLL targets SET domain methyltransferase activity to Hox gene promoters. Mol. Cell 10:1107-1117

Miranda T.B., Sayegh J., Frankel A., Katz J.E., Miranda M., and Clarke S., 2006. Yeast Hsl7 (histone synthetic lethal 7) catalyses the in vitro formation of co-N G-monomethylarginine in calf thymus histone H2A. Biochem. J. 395:563-570.

Mizzen C.A., Yang X.J., Kokubo T., Brownell J.E., Bannister A.J., Owen-Hughes T.. Workman J.. Wang L., Berger S.L., Kouzarides T., et al., 1996. The TAF n250 subunit of TFIID has histone acetyltransferase activity. Cell 87: 1261-1270.

Morris S.A., Shibata Y., Noma K., Tsukamoto Y., Warren E., Temple B., Grewal S.L, and Strahl B.D., 2005. Histone H3 K36 methylation is associated with transcription elongation in Schizosac-charomyces pombe. Eukaryot. Cell 4: 1446-1454.

Mukheijee B., Kessinger C., Kobayashi J., Chen B.P., Chen D.J., Chatteijee A, and Burma S., 2006. DNA-PK phosphorylates histone H2AX during apoptotic DNA fragmentation in mammalian cells. DNA Repair 5:575-590.

Muller J., Hart CM., Francis N.J., Vargas M.L., Sengupta A., Wild B., Miller E.L., O’Connor M.B., Kingston R.E., and Simon J.A., 2002. Histone methyltransferase activity of a Drosophila Polycomb group repressor complex. Cell 111: 197-208.

Nagy P.L., Griesenbeck J., Komberg R.D., and Cleary M.L., 2002. A trithorax-group complex purified from Saccharomyces cerevisiae is required for methylation of histone H3. Proc. Natl. Acad. Sci. 99: 90-94.

Nakamura T., Mori T., Tada S., Krajewski W., Rozovskaia T., Wassell R., Dubois G., Mazo A., Croce C.M., and Canaani E., 2002. ALL-1 is a histone methyltransferase that assembles a supercomplex of proteins involved in transcriptional regulation. Mol. Cell 10:1119-1128.

Nakayama J., Rice J.C., Strahl B.D., Allis C.D., and Grewal S.L, 2001. Role of histone H3 lysine 9 methylation in epigenetic control of heterochromatin assembly. Science 292:110—113.

Nathan D., Ingvarsdottir K., Sterner D.E., Bylebyl G.R., Dok-manovic M., Dorsey J.A., Whelan K.A., Krsmanovic M., Lane W.S., Meluh P.B., et al., 2006. Histone sumoylation is a negative regulator in Saccharomyces cerevisiae and shows dynamic interplay with positive-acting histone modifications. Genes Dev., 20:966-976.

Ng H.H., Xu R.M., Zhang Y., and Struhl K., 2002. Ubiquitination of histone H2B by Rad6 is required for efficient Dot 1 -mediated methylation of histone H3 lysine 79. J. Biol. Chem. 277: 34655-34657.

Nielsen S.J., Schneider R., Bauer U.M., Bannister A.J., Morrison A., O’Carroll D., Firestein R., Cleary M., Jenuwein T., Herrera R.E., and Kouzarides T., 2001. Rb targets histone H3 methylation and HP1 to promoters. Nature 412:561-565.

Nishioka K., Chuikov S., Sarma K., Erdjument-Bromage H., Allis C.D., Tempst P., and Reinberg D., 2002a. Set9, a novel histone H3 methyltransferase that facilitates transcription by precluding histone tail modifications required for heterochromatin formation. Genes Dev. 16:479-489.

Nishioka K., Rice J.C., Sarma K., Erdjument-Bromage H, Werner J., Wang Y., Chuikov S., Valenzuela P., Tempst P., Steward R., et al., 2002. PR-Set7 is a nucleosome-specific methyltransferase that modifies lysine, 20 of histone H4 and is associated with silent chromatin. Mol. Cell 9: 1201-1213.

Nowak S.J. and Corces V.G., 2000. Phosphorylation of histone H3 correlates with transcriptionally active loci. Genes Dev. 14:3003-3013.