Продукт гена HDAC2 относится к семейству деацетилаз гистонов. Гистондеацетилазы работают в составе крупных мультибелковых комплексов и отвечают за деацетилирование остатков лизина на N-концевой области кóровых гистонов (H2A, H2B, H3 и H4). Этот белок также формирует комплексы транскрипционных репрессоров, связываясь с различными белками, в том числе YY1, одним из фактором транскрипции млекопитающих. Гистондеацетилаза 2 играет важную роль в регуляции транскрипции, клеточного цикла и в развитии.[2]
1 2 Schmidt DR, Schreiber SL. “Molecular association between ATR and two components of the nucleosome remodeling and deacetylating complex, HDAC2 and CHD4”. Biochemistry. 38 (44): 14711–7. DOI:10.1021/bi991614n. PMID10545197.
1 2 3 4 Yoon YM, Baek KH, Jeong SJ, Shin HJ, Ha GH, Jeon AH, Hwang SG, Chun JS, Lee CW. “WD repeat-containing mitotic checkpoint proteins act as transcriptional repressors during interphase”. FEBS Lett. 575 (1–3): 23–9. DOI:10.1016/j.febslet.2004.07.089. PMID15388328.
1 2 3 4 5 6 7 8 9 10 Hakimi MA, Dong Y, Lane WS, Speicher DW, Shiekhattar R. “A candidate X-linked mental retardation gene is a component of a new family of histone deacetylase-containing complexes”. J. Biol. Chem. 278 (9): 7234–9. DOI:10.1074/jbc.M208992200. PMID12493763.
1 2 3 4 5 Tong JK, Hassig CA, Schnitzler GR, Kingston RE, Schreiber SL. “Chromatin deacetylation by an ATP-dependent nucleosome remodelling complex”. Nature. 395 (6705): 917–21. DOI:10.1038/27699. PMID9804427.
1 2 Hakimi MA, Bochar DA, Schmiesing JA, Dong Y, Barak OG, Speicher DW, Yokomori K, Shiekhattar R. “A chromatin remodelling complex that loads cohesin onto human chromosomes”. Nature. 418 (6901): 994–8. DOI:10.1038/nature01024. PMID12198550.
↑ Rountree MR, Bachman KE, Baylin SB. “DNMT1 binds HDAC2 and a new co-repressor, DMAP1, to form a complex at replication foci”. Nat. Genet. 25 (3): 269–77. DOI:10.1038/77023. PMID10888872.
1 2 3 van der Vlag J, Otte AP. “Transcriptional repression mediated by the human polycomb-group protein EED involves histone deacetylation”. Nat. Genet. 23 (4): 474–8. DOI:10.1038/70602. PMID10581039.
↑ Wen YD, Cress WD, Roy AL, Seto E. “Histone deacetylase 3 binds to and regulates the multifunctional transcription factor TFII-I”. J. Biol. Chem. 278 (3): 1841–7. DOI:10.1074/jbc.M206528200. PMID12393887.
1 2 Fischer DD, Cai R, Bhatia U, Asselbergs FA, Song C, Terry R, Trogani N, Widmer R, Atadja P, Cohen D. “Isolation and characterization of a novel class II histone deacetylase, HDAC10”. J. Biol. Chem. 277 (8): 6656–66. DOI:10.1074/jbc.M108055200. PMID11739383.
1 2 3 Yao YL, Yang WM. “The metastasis-associated proteins 1 and 2 form distinct protein complexes with histone deacetylase activity”. J. Biol. Chem. 278 (43): 42560–8. DOI:10.1074/jbc.M302955200. PMID12920132.
1 2 Johnson CA, White DA, Lavender JS, O'Neill LP, Turner BM. “Human class I histone deacetylase complexes show enhanced catalytic activity in the presence of ATP and co-immunoprecipitate with the ATP-dependent chaperone protein Hsp70”. J. Biol. Chem. 277 (11): 9590–7. DOI:10.1074/jbc.M107942200. PMID11777905.
↑ Fischle W, Dequiedt F, Hendzel MJ, Guenther MG, Lazar MA, Voelter W, Verdin E. “Enzymatic activity associated with class II HDACs is dependent on a multiprotein complex containing HDAC3 and SMRT/N-CoR”. Mol. Cell. 9 (1): 45–57. DOI:10.1016/s1097-2765(01)00429-4. PMID11804585.
↑ Fischle W, Dequiedt F, Fillion M, Hendzel MJ, Voelter W, Verdin E. “Human HDAC7 histone deacetylase activity is associated with HDAC3 in vivo”. J. Biol. Chem. 276 (38): 35826–35. DOI:10.1074/jbc.M104935200. PMID11466315.
↑ Zhang Y, Iratni R, Erdjument-Bromage H, Tempst P, Reinberg D. “Histone deacetylases and SAP18, a novel polypeptide, are components of a human Sin3 complex”. Cell. 89 (3): 357–64. DOI:10.1016/s0092-8674(00)80216-0. PMID9150135.
↑ Mazumdar A, Wang RA, Mishra SK, Adam L, Bagheri-Yarmand R, Mandal M, Vadlamudi RK, Kumar R. “Transcriptional repression of oestrogen receptor by metastasis-associated protein 1 corepressor”. Nat. Cell Biol. 3 (1): 30–7. DOI:10.1038/35050532. PMID11146623.
1 2 Laherty CD, Yang WM, Sun JM, Davie JR, Seto E, Eisenman RN. “Histone deacetylases associated with the mSin3 corepressor mediate mad transcriptional repression”. Cell. 89 (3): 349–56. DOI:10.1016/s0092-8674(00)80215-9. PMID9150134.
↑ Spronk CA, Tessari M, Kaan AM, Jansen JF, Vermeulen M, Stunnenberg HG, Vuister GW. “The Mad1-Sin3B interaction involves a novel helical fold”. Nat. Struct. Biol. 7 (12): 1100–4. DOI:10.1038/81944. PMID11101889.
↑ Brackertz M, Boeke J, Zhang R, Renkawitz R. “Two highly related p66 proteins comprise a new family of potent transcriptional repressors interacting with MBD2 and MBD3”. J. Biol. Chem. 277 (43): 40958–66. DOI:10.1074/jbc.M207467200. PMID12183469.
↑ Ng HH, Zhang Y, Hendrich B, Johnson CA, Turner BM, Erdjument-Bromage H, Tempst P, Reinberg D, Bird A. “MBD2 is a transcriptional repressor belonging to the MeCP1 histone deacetylase complex”. Nat. Genet. 23 (1): 58–61. DOI:10.1038/12659. PMID10471499.
↑ Iwase S, Januma A, Miyamoto K, Shono N, Honda A, Yanagisawa J, Baba T. “Characterization of BHC80 in BRAF-HDAC complex, involved in neuron-specific gene repression”. Biochem. Biophys. Res. Commun. 322 (2): 601–8. DOI:10.1016/j.bbrc.2004.07.163. PMID15325272.
↑ Jin Q, van Eynde A, Beullens M, Roy N, Thiel G, Stalmans W, Bollen M. “The protein phosphatase-1 (PP1) regulator, nuclear inhibitor of PP1 (NIPP1), interacts with the polycomb group protein, embryonic ectoderm development (EED), and functions as a transcriptional repressor”. J. Biol. Chem. 278 (33): 30677–85. DOI:10.1074/jbc.M302273200. PMID12788942.
1 2 Zhang Y, Dufau ML. “Dual mechanisms of regulation of transcription of luteinizing hormone receptor gene by nuclear orphan receptors and histone deacetylase complexes”. J. Steroid Biochem. Mol. Biol. 85 (2–5): 401–14. DOI:10.1016/s0960-0760(03)00230-9. PMID12943729.
1 2 3 Zhang Y, Dufau ML. “Silencing of transcription of the human luteinizing hormone receptor gene by histone deacetylase-mSin3A complex”. J. Biol. Chem. 277 (36): 33431–8. DOI:10.1074/jbc.M204417200. PMID12091390.
↑ Kiernan R, Brès V, Ng RW, Coudart MP, El Messaoudi S, Sardet C, Jin DY, Emiliani S, Benkirane M. “Post-activation turn-off of NF-kappa B-dependent transcription is regulated by acetylation of p65”. J. Biol. Chem. 278 (4): 2758–66. DOI:10.1074/jbc.M209572200. PMID12419806.
↑ Zhang Y, Sun ZW, Iratni R, Erdjument-Bromage H, Tempst P, Hampsey M, Reinberg D. “SAP30, a novel protein conserved between human and yeast, is a component of a histone deacetylase complex”. Mol. Cell. 1 (7): 1021–31. DOI:10.1016/s1097-2765(00)80102-1. PMID9651585.
1 2 Won J, Yim J, Kim TK. “Sp1 and Sp3 recruit histone deacetylase to repress transcription of human telomerase reverse transcriptase (hTERT) promoter in normal human somatic cells”. J. Biol. Chem. 277 (41): 38230–8. DOI:10.1074/jbc.M206064200. PMID12151407.
1 2 Sun JM, Chen HY, Moniwa M, Litchfield DW, Seto E, Davie JR. “The transcriptional repressor Sp3 is associated with CK2-phosphorylated histone deacetylase 2”. J. Biol. Chem. 277 (39): 35783–6. DOI:10.1074/jbc.C200378200. PMID12176973.
↑ Tsai SC, Valkov N, Yang WM, Gump J, Sullivan D, Seto E. “Histone deacetylase interacts directly with DNA topoisomerase II”. Nat. Genet. 26 (3): 349–53. DOI:10.1038/81671. PMID11062478.
↑ Yang WM, Yao YL, Sun JM, Davie JR, Seto E. “Isolation and characterization of cDNAs corresponding to an additional member of the human histone deacetylase gene family”. J. Biol. Chem. 272 (44): 28001–7. DOI:10.1074/jbc.272.44.28001. PMID9346952.
Zhang Y, Dufau ML (2003). “Dual mechanisms of regulation of transcription of luteinizing hormone receptor gene by nuclear orphan receptors and histone deacetylase complexes”. J. Steroid Biochem. Mol. Biol. 85 (2—5): 401—14. DOI:10.1016/S0960-0760(03)00230-9. PMID12943729.
Furukawa Y, Kawakami T, Sudo K, Inazawa J, Matsumine A, Akiyama T, Nakamura Y (1996). “Isolation and mapping of a human gene (RPD3L1) that is homologous to RPD3, a transcription factor in Saccharomyces cerevisiae”. Cytogenet. Cell Genet. 73 (1—2): 130—3. DOI:10.1159/000134323. PMID8646880.
Laherty CD, Yang WM, Sun JM, Davie JR, Seto E, Eisenman RN (1997). “Histone deacetylases associated with the mSin3 corepressor mediate mad transcriptional repression”. Cell. 89 (3): 349—56. DOI:10.1016/S0092-8674(00)80215-9. PMID9150134.
Zhang Y, Iratni R, Erdjument-Bromage H, Tempst P, Reinberg D (1997). “Histone deacetylases and SAP18, a novel polypeptide, are components of a human Sin3 complex”. Cell. 89 (3): 357—64. DOI:10.1016/S0092-8674(00)80216-0. PMID9150135.
Yang WM, Yao YL, Sun JM, Davie JR, Seto E (1997). “Isolation and characterization of cDNAs corresponding to an additional member of the human histone deacetylase gene family”. J. Biol. Chem. 272 (44): 28001—7. DOI:10.1074/jbc.272.44.28001. PMID9346952.
Randhawa GS, Bell DW, Testa JR, Feinberg AP (1998). “Identification and mapping of human histone acetylation modifier gene homologues”. Genomics. 51 (2): 262—9. DOI:10.1006/geno.1998.5370. PMID9722949.
Zhang Y, LeRoy G, Seelig HP, Lane WS, Reinberg D (1998). “The dermatomyositis-specific autoantigen Mi2 is a component of a complex containing histone deacetylase and nucleosome remodeling activities”. Cell. 95 (2): 279—89. DOI:10.1016/S0092-8674(00)81758-4. PMID9790534.
Tong JK, Hassig CA, Schnitzler GR, Kingston RE, Schreiber SL (1998). “Chromatin deacetylation by an ATP-dependent nucleosome remodelling complex”. Nature. 395 (6705): 917—21. DOI:10.1038/27699. PMID9804427.
Ng HH, Zhang Y, Hendrich B, Johnson CA, Turner BM, Erdjument-Bromage H, Tempst P, Reinberg D, Bird A (1999). “MBD2 is a transcriptional repressor belonging to the MeCP1 histone deacetylase complex”. Nat. Genet. 23 (1): 58—61. DOI:10.1038/12659. PMID10471499.
Wade PA, Gegonne A, Jones PL, Ballestar E, Aubry F, Wolffe AP (1999). “Mi-2 complex couples DNA methylation to chromatin remodelling and histone deacetylation”. Nat. Genet. 23 (1): 62—6. DOI:10.1038/12664. PMID10471500.
Другой контент может иметь иную лицензию. Перед использованием материалов сайта WikiSort.ru внимательно изучите правила лицензирования конкретных элементов наполнения сайта.
2019-2025 WikiSort.ru - проект по пересортировке и дополнению контента Википедии