Гистондеацетилаза 2

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Гистондеацетилаза 2
Доступные структуры
PDB Поиск ортологов: PDBe, RCSB
Идентификаторы
Символ HDAC2 ; HD2; RPD3; YAF1
Внешние ID OMIM: 605164 MGI1097691 HomoloGene68187 ChEMBL: 1937 GeneCards: HDAC2 Gene
номер EC 3.5.1.98
Профиль экспрессии РНК
PBB GE HDAC2 201833 at tn.png
Больше информации
Ортологи
Вид Человек Мышь
Entrez 3066 15182
Ensembl ENSG00000196591 ENSMUSG00000019777
UniProt Q92769 P70288
RefSeq (мРНК) NM_001527 NM_008229
RefSeq (белок) NP_001518 NP_032255
Локус (UCSC) Chr 6:
114.25 – 114.33 Mb
Chr 10:
36.97 – 37 Mb
Поиск в PubMed [1] [2]

Гистондеацетилаза 2  — фермент из семейства деацетилаз гистонов, кодируемый у человека геном HDAC2 .[1]

Функция[править | править код]

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]

Взаимодействия[править | править код]

Гистондезацетилаза 2 взаимодействует с:

Примечания[править | править код]

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  2. Entrez Gene: HDAC2 histone deacetylase 2.
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  7. 1 2 «A chromatin remodelling complex that loads cohesin onto human chromosomes». Nature 418 (6901): 994-8. DOI:10.1038/nature01024. PMID 12198550.
  8. «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. PMID 10888872.
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  11. Three-way control of fetal heart-cell proliferation could help regenerate cardiac cells (October 7, 2010).
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  15. 1 2 3 4 «A core-BRAF35 complex containing histone deacetylase mediates repression of neuronal-specific genes». Proc. Natl. Acad. Sci. U.S.A. 99 (11): 7420-5. DOI:10.1073/pnas.112008599. PMID 12032298.
  16. 1 2 «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. PMID 11777905.
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  19. «The p65 (RelA) subunit of NF-kappaB interacts with the histone deacetylase (HDAC) corepressors HDAC1 and HDAC2 to negatively regulate gene expression». Mol. Cell. Biol. 21 (20): 7065-77. DOI:10.1128/MCB.21.20.7065-7077.2001. PMID 11564889.
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  22. «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. PMID 9150135.
  23. «Human Sin3 deacetylase and trithorax-related Set1/Ash2 histone H3-K4 methyltransferase are tethered together selectively by the cell-proliferation factor HCF-1». Genes Dev. 17 (7): 896-911. DOI:10.1101/gad.252103. PMID 12670868.
  24. «Transcriptional repression of oestrogen receptor by metastasis-associated protein 1 corepressor». Nat. Cell Biol. 3 (1): 30-7. DOI:10.1038/35050532. PMID 11146623.
  25. 1 2 «Histone deacetylases associated with the mSin3 corepressor mediate mad transcriptional repression». Cell 89 (3): 349-56. DOI:10.1016/s0092-8674(00)80215-9. PMID 9150134.
  26. «The Mad1-Sin3B interaction involves a novel helical fold». Nat. Struct. Biol. 7 (12): 1100-4. DOI:10.1038/81944. PMID 11101889.
  27. «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. PMID 12183469.
  28. «MBD2 is a transcriptional repressor belonging to the MeCP1 histone deacetylase complex». Nat. Genet. 23 (1): 58-61. DOI:10.1038/12659. PMID 10471499.
  29. «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. PMID 15325272.
  30. «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. PMID 12788942.
  31. 1 2 «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. PMID 12943729.
  32. 1 2 3 «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. PMID 12091390.
  33. «CoREST is an integral component of the CoREST- human histone deacetylase complex». Proc. Natl. Acad. Sci. U.S.A. 98 (4): 1454-8. DOI:10.1073/pnas.98.4.1454. PMID 11171972.
  34. «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. PMID 12419806.
  35. «Histone deacetylases augment cytokine induction of the iNOS gene». J. Am. Soc. Nephrol. 13 (8): 2009-17. DOI:10.1097/01.asn.0000024253.59665.f1. PMID 12138131.
  36. «RBP1 recruits both histone deacetylase-dependent and -independent repression activities to retinoblastoma family proteins». Mol. Cell. Biol. 19 (10): 6632-41. PMID 10490602.
  37. «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. PMID 9651585.
  38. «Role of the Sin3-histone deacetylase complex in growth regulation by the candidate tumor suppressor p33(ING1)». Mol. Cell. Biol. 22 (3): 835-48. DOI:10.1128/mcb.22.3.835-848.2002. PMID 11784859.
  39. «Identification and characterization of three new components of the mSin3A corepressor complex». Mol. Cell. Biol. 23 (10): 3456-67. DOI:10.1128/mcb.23.10.3456-3467.2003. PMID 12724404.
  40. «An ERG (ets-related gene)-associated histone methyltransferase interacts with histone deacetylases 1/2 and transcription co-repressors mSin3A/B». Biochem. J. 369 (Pt 3): 651-7. DOI:10.1042/BJ20020854. PMID 12398767.
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  42. «Functional and physical interaction between the histone methyl transferase Suv39H1 and histone deacetylases». Nucleic Acids Res. 30 (2): 475-81. DOI:10.1093/nar/30.2.475. PMID 11788710.
  43. 1 2 «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. PMID 12151407.
  44. 1 2 «The transcriptional repressor Sp3 is associated with CK2-phosphorylated histone deacetylase 2». J. Biol. Chem. 277 (39): 35783-6. DOI:10.1074/jbc.C200378200. PMID 12176973.
  45. «Histone deacetylase interacts directly with DNA topoisomerase II». Nat. Genet. 26 (3): 349-53. DOI:10.1038/81671. PMID 11062478.
  46. «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. PMID 9346952.
  47. «Regulation of transcription factor YY1 by acetylation and deacetylation». Mol. Cell. Biol. 21 (17): 5979-91. DOI:10.1128/mcb.21.17.5979-5991.2001. PMID 11486036.
  48. «Yeast two-hybrid cloning of a novel zinc finger protein that interacts with the multifunctional transcription factor YY1». Nucleic Acids Res. 25 (4): 843-9. DOI:10.1093/nar/25.4.843. PMID 9016636.

Литература[править | править код]

  • (2000) «NuRD and SIN3 histone deacetylase complexes in development». Trends Genet. 16 (8): 351–6. DOI:10.1016/S0168-9525(00)02066-7. PMID 10904264.
  • (2003) «Class II histone deacetylases: versatile regulators». Trends Genet. 19 (5): 286–93. DOI:10.1016/S0168-9525(03)00073-8. PMID 12711221.
  • (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. PMID 12943729.
  • (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. PMID 8646880.
  • (1996) «Transcriptional repression by YY1 is mediated by interaction with a mammalian homolog of the yeast global regulator RPD3». Proc. Natl. Acad. Sci. U.S.A. 93 (23): 12845–50. DOI:10.1073/pnas.93.23.12845. PMID 8917507.
  • (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. PMID 9150134.
  • (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. PMID 9150135.
  • (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. PMID 9346952.
  • (1998) «A role for histone deacetylase activity in HDAC1-mediated transcriptional repression». Proc. Natl. Acad. Sci. U.S.A. 95 (7): 3519–24. DOI:10.1073/pnas.95.7.3519. PMID 9520398.
  • (1998) «Identification and mapping of human histone acetylation modifier gene homologues». Genomics 51 (2): 262–9. DOI:10.1006/geno.1998.5370. PMID 9722949.
  • (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. PMID 9790534.
  • (1998) «Chromatin deacetylation by an ATP-dependent nucleosome remodelling complex». Nature 395 (6705): 917–21. DOI:10.1038/27699. PMID 9804427.
  • (1999) «CIR, a corepressor linking the DNA binding factor CBF1 to the histone deacetylase complex». Proc. Natl. Acad. Sci. U.S.A. 96 (1): 23–8. DOI:10.1073/pnas.96.1.23. PMID 9874765.
  • (1999) «BRCA1 interacts with components of the histone deacetylase complex». Proc. Natl. Acad. Sci. U.S.A. 96 (9): 4983–8. DOI:10.1073/pnas.96.9.4983. PMID 10220405.
  • (1999) «Repression by Ikaros and Aiolos is mediated through histone deacetylase complexes». EMBO J. 18 (11): 3090–100. DOI:10.1093/emboj/18.11.3090. PMID 10357820.
  • (1999) «Analysis of the NuRD subunits reveals a histone deacetylase core complex and a connection with DNA methylation». Genes Dev. 13 (15): 1924–35. DOI:10.1101/gad.13.15.1924. PMID 10444591.
  • (1999) «MBD2 is a transcriptional repressor belonging to the MeCP1 histone deacetylase complex». Nat. Genet. 23 (1): 58–61. DOI:10.1038/12659. PMID 10471499.
  • (1999) «Mi-2 complex couples DNA methylation to chromatin remodelling and histone deacetylation». Nat. Genet. 23 (1): 62–6. DOI:10.1038/12664. PMID 10471500.
  • (2000) «RBP1 Recruits Both Histone Deacetylase-Dependent and -Independent Repression Activities to Retinoblastoma Family Proteins». Mol. Cell. Biol. 19 (10): 6632–41. PMID 10490602.