Biology:HDAC1
From HandWiki
Histone deacetylase 1 (HDAC1) is an enzyme that in humans is encoded by the HDAC1 gene.[1]
Function
Histone acetylation and deacetylation, catalyzed by multisubunit complexes, play a key role in the regulation of eukaryotic gene expression. The protein encoded by this gene belongs to the histone deacetylase/acuc/apha family and is a component of the histone deacetylase complex. It also interacts with retinoblastoma tumor-suppressor protein and this complex is a key element in the control of cell proliferation and differentiation. Together with metastasis-associated protein-2 MTA2, it deacetylates p53 and modulates its effect on cell growth and apoptosis.[2]
Interactions
HDAC1 has been shown to interact with:
- Androgen receptor,[3]
- BCL6,[4][5]
- BTG2,[6][7]
- BUB1B,[8]
- BUB1,[8]
- BUB3,[8]
- CBFA2T3,[9][10]
- CDC20,[8]
- CDH1,[8]
- CHD3,[11][12]
- CHD4,[11][13][14]
- COUP-TFII,[15]
- CTBP1,[16][17][18]
- DDX17,[19]
- DDX5,[19]
- DNMT3A,[20]
- DNMT3L,[21][22]
- Death-associated protein 6,[23]
- EED,[24]
- EVI1,[25][26]
- EZH2,[24]
- FKBP3,[27]
- GATA1,[28]
- HMG20B,[29]
- HSPA4,[30]
- HUS1,[31]
- Histone deacetylase 2,[11][13][24][29][30][32][33][34][35][36][37][38][39]
- Homeobox protein TGIF1,[16][40]
- Host cell factor C1,[41]
- IFRD1,[42]
- IKZF1,[43][44]
- ING1,[12][45]
- MBD3,[37][46][47]
- MIER1,[48]
- MLL,[49]
- MTA1,[13][50]
- MTA2,[13][37][51][52]
- Mad1,[8]
- Mdm2,[53]
- Methyl-CpG-binding domain protein 2,[37][54][55]
- Mothers against decapentaplegic homolog 2,[56]
- MyoD,[57][58]
- NFKB1,[59]
- Nuclear receptor co-repressor 2,[32][60]
- P21,[61]
- PCNA,[62]
- PHF21A,[29][63]
- Prohibitin,[64][65]
- Promyelocytic leukemia protein,[66][67]
- RAD9A,[31]
- RBBP4,[13][14][37][38][39][51][54][68][69][70][71]
- RBBP7,[13][37][39][54]
- RCOR1,[29][51]
- RELA,[36][59][72]
- RFC1,[73]
- Retinoblastoma protein,[57][65][74][75][76][77][78]
- Retinoblastoma-like protein 1,[74][75]
- Retinoblastoma-like protein 2,[74][79]
- SAP30,[12][37][80][81][82][83]
- SATB1,[52]
- SIN3A,[11][12][13][14][37][38][51][52][68][69][84][85][86][87]
- SIN3B,[37][43]
- SPEN,[88]
- SUDS3,[84][89]
- SUV39H1,[90]
- Sp1 transcription factor,[69][91][92][93]
- TOP2A,[94][95]
- TOP2B,[94][95] and
- Zinc finger and BTB domain-containing protein 16.[4][96][97]
See also
References
- ↑ "A mammalian histone deacetylase related to the yeast transcriptional regulator Rpd3p". Science (New York, N.Y.) 272 (5260): 408–411. April 1996. doi:10.1126/science.272.5260.408. PMID 8602529. Bibcode: 1996Sci...272..408T.
- ↑ "Entrez Gene: HDAC1 histone deacetylase 1". https://www.ncbi.nlm.nih.gov/gene?Db=gene&Cmd=ShowDetailView&TermToSearch=3065.
- ↑ "Tip60 and histone deacetylase 1 regulate androgen receptor activity through changes to the acetylation status of the receptor". The Journal of Biological Chemistry 277 (29): 25904–25913. July 2002. doi:10.1074/jbc.M203423200. PMID 11994312.
- ↑ 4.0 4.1 "Histone deacetylase associated with mSin3A mediates repression by the acute promyelocytic leukemia-associated PLZF protein". Oncogene 16 (19): 2549–2556. May 1998. doi:10.1038/sj.onc.1202043. PMID 9627120.
- ↑ "Recruitment of SMRT/N-CoR-mSin3A-HDAC-repressing complexes is not a general mechanism for BTB/POZ transcriptional repressors: the case of HIC-1 and gammaFBP-B". Proceedings of the National Academy of Sciences of the United States of America 96 (26): 14831–14836. December 1999. doi:10.1073/pnas.96.26.14831. PMID 10611298. Bibcode: 1999PNAS...9614831D.
- ↑ "Inhibition of medulloblastoma tumorigenesis by the antiproliferative and pro-differentiative gene PC3". FASEB Journal 21 (9): 2215–2225. July 2007. doi:10.1096/fj.06-7548com. PMID 17371797.
- ↑ "HDAC1, HDAC4, and HDAC9 Bind to PC3/Tis21/Btg2 and Are Required for Its Inhibition of Cell Cycle Progression and Cyclin D1 Expression". Journal of Cellular Physiology 232 (7): 1696–1707. July 2017. doi:10.1002/jcp.25467. PMID 27333946. http://www.inmm.cnr.it/tirone/pdfs/Micheli_et_al-2017-J_Cell_Physiol%20PC3-HDACs.pdf.
- ↑ 8.0 8.1 8.2 8.3 8.4 8.5 "WD repeat-containing mitotic checkpoint proteins act as transcriptional repressors during interphase". FEBS Letters 575 (1–3): 23–29. September 2004. doi:10.1016/j.febslet.2004.07.089. PMID 15388328. Bibcode: 2004FEBSL.575...23Y.
- ↑ "The transcriptional corepressor MTG16a contains a novel nucleolar targeting sequence deranged in t (16; 21)-positive myeloid malignancies". Oncogene 21 (43): 6703–6712. September 2002. doi:10.1038/sj.onc.1205882. PMID 12242670.
- ↑ "ETO, a target of t(8;21) in acute leukemia, makes distinct contacts with multiple histone deacetylases and binds mSin3A through its oligomerization domain". Molecular and Cellular Biology 21 (19): 6470–6483. October 2001. doi:10.1128/mcb.21.19.6470-6483.2001. PMID 11533236.
- ↑ 11.0 11.1 11.2 11.3 "Chromatin deacetylation by an ATP-dependent nucleosome remodelling complex". Nature 395 (6705): 917–921. October 1998. doi:10.1038/27699. PMID 9804427. Bibcode: 1998Natur.395..917T.
- ↑ 12.0 12.1 12.2 12.3 "Role of the Sin3-histone deacetylase complex in growth regulation by the candidate tumor suppressor p33(ING1)". Molecular and Cellular Biology 22 (3): 835–848. February 2002. doi:10.1128/mcb.22.3.835-848.2002. PMID 11784859.
- ↑ 13.0 13.1 13.2 13.3 13.4 13.5 13.6 "The metastasis-associated proteins 1 and 2 form distinct protein complexes with histone deacetylase activity". The Journal of Biological Chemistry 278 (43): 42560–42568. October 2003. doi:10.1074/jbc.M302955200. PMID 12920132.
- ↑ 14.0 14.1 14.2 "Three proteins define a class of human histone deacetylases related to yeast Hda1p". Proceedings of the National Academy of Sciences of the United States of America 96 (9): 4868–4873. April 1999. doi:10.1073/pnas.96.9.4868. PMID 10220385. Bibcode: 1999PNAS...96.4868G.
- ↑ "Association of histone deacetylase with COUP-TF in tumorigenic Ad12-transformed cells and its potential role in shut-off of MHC class I transcription". Virology 268 (2): 319–328. March 2000. doi:10.1006/viro.1999.0181. PMID 10704340.
- ↑ 16.0 16.1 "The interaction of the carboxyl terminus-binding protein with the Smad corepressor TGIF is disrupted by a holoprosencephaly mutation in TGIF". The Journal of Biological Chemistry 275 (50): 39762–39766. December 2000. doi:10.1074/jbc.C000416200. PMID 10995736.
- ↑ "Association of COOH-terminal-binding protein (CtBP) and MEF2-interacting transcription repressor (MITR) contributes to transcriptional repression of the MEF2 transcription factor". The Journal of Biological Chemistry 276 (1): 35–39. January 2001. doi:10.1074/jbc.M007364200. PMID 11022042.
- ↑ "The carboxy-terminal region of adenovirus E1A activates transcription through targeting of a C-terminal binding protein-histone deacetylase complex". FEBS Letters 429 (2): 183–188. June 1998. doi:10.1016/s0014-5793(98)00588-2. PMID 9650586. Bibcode: 1998FEBSL.429..183S.
- ↑ 19.0 19.1 "The p68 and p72 DEAD box RNA helicases interact with HDAC1 and repress transcription in a promoter-specific manner". BMC Molecular Biology 5. August 2004. doi:10.1186/1471-2199-5-11. PMID 15298701.
- ↑ "Dnmt3a binds deacetylases and is recruited by a sequence-specific repressor to silence transcription". The EMBO Journal 20 (10): 2536–2544. May 2001. doi:10.1093/emboj/20.10.2536. PMID 11350943.
- ↑ "Imprinting regulator DNMT3L is a transcriptional repressor associated with histone deacetylase activity". Nucleic Acids Research 30 (16): 3602–3608. August 2002. doi:10.1093/nar/gkf474. PMID 12177302.
- ↑ "Dnmt3L is a transcriptional repressor that recruits histone deacetylase". Nucleic Acids Research 30 (17): 3831–3838. September 2002. doi:10.1093/nar/gkf509. PMID 12202768.
- ↑ "Sequestration and inhibition of Daxx-mediated transcriptional repression by PML". Molecular and Cellular Biology 20 (5): 1784–1796. March 2000. doi:10.1128/mcb.20.5.1784-1796.2000. PMID 10669754.
- ↑ 24.0 24.1 24.2 "Transcriptional repression mediated by the human polycomb-group protein EED involves histone deacetylation". Nature Genetics 23 (4): 474–478. December 1999. doi:10.1038/70602. PMID 10581039.
- ↑ "The leukaemia-associated transcription factors EVI-1 and MDS1/EVI1 repress transcription and interact with histone deacetylase". British Journal of Haematology 114 (3): 566–573. September 2001. doi:10.1046/j.1365-2141.2001.02987.x. PMID 11552981.
- ↑ "Interaction of EVI1 with cAMP-responsive element-binding protein-binding protein (CBP) and p300/CBP-associated factor (P/CAF) results in reversible acetylation of EVI1 and in co-localization in nuclear speckles". The Journal of Biological Chemistry 276 (48): 44936–44943. November 2001. doi:10.1074/jbc.M106733200. PMID 11568182.
- ↑ "The FK506-binding protein 25 functionally associates with histone deacetylases and with transcription factor YY1". The EMBO Journal 20 (17): 4814–4825. September 2001. doi:10.1093/emboj/20.17.4814. PMID 11532945.
- ↑ "Altered interaction of HDAC5 with GATA-1 during MEL cell differentiation". Oncogene 22 (57): 9176–9184. December 2003. doi:10.1038/sj.onc.1206902. PMID 14668799.
- ↑ 29.0 29.1 29.2 29.3 "A core-BRAF35 complex containing histone deacetylase mediates repression of neuronal-specific genes". Proceedings of the National Academy of Sciences of the United States of America 99 (11): 7420–7425. May 2002. doi:10.1073/pnas.112008599. PMID 12032298. Bibcode: 2002PNAS...99.7420H.
- ↑ 30.0 30.1 "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". The Journal of Biological Chemistry 277 (11): 9590–9597. March 2002. doi:10.1074/jbc.M107942200. PMID 11777905.
- ↑ 31.0 31.1 "HDAC1, a histone deacetylase, forms a complex with Hus1 and Rad9, two G2/M checkpoint Rad proteins". The Journal of Biological Chemistry 275 (36): 27909–27916. September 2000. doi:10.1074/jbc.M000168200. PMID 10846170.
- ↑ 32.0 32.1 "Isolation and characterization of a novel class II histone deacetylase, HDAC10". The Journal of Biological Chemistry 277 (8): 6656–6666. February 2002. doi:10.1074/jbc.M108055200. PMID 11739383.
- ↑ "A candidate X-linked mental retardation gene is a component of a new family of histone deacetylase-containing complexes". The Journal of Biological Chemistry 278 (9): 7234–7239. February 2003. doi:10.1074/jbc.M208992200. PMID 12493763.
- ↑ "Enzymatic activity associated with class II HDACs is dependent on a multiprotein complex containing HDAC3 and SMRT/N-CoR". Molecular Cell 9 (1): 45–57. January 2002. doi:10.1016/s1097-2765(01)00429-4. PMID 11804585.
- ↑ "Human HDAC7 histone deacetylase activity is associated with HDAC3 in vivo". The Journal of Biological Chemistry 276 (38): 35826–35835. September 2001. doi:10.1074/jbc.M104935200. PMID 11466315.
- ↑ 36.0 36.1 "The p65 (RelA) subunit of NF-kappaB interacts with the histone deacetylase (HDAC) corepressors HDAC1 and HDAC2 to negatively regulate gene expression". Molecular and Cellular Biology 21 (20): 7065–7077. October 2001. doi:10.1128/MCB.21.20.7065-7077.2001. PMID 11564889.
- ↑ 37.0 37.1 37.2 37.3 37.4 37.5 37.6 37.7 37.8 "Analysis of the NuRD subunits reveals a histone deacetylase core complex and a connection with DNA methylation". Genes & Development 13 (15): 1924–1935. August 1999. doi:10.1101/gad.13.15.1924. PMID 10444591.
- ↑ 38.0 38.1 38.2 "A role for histone deacetylase activity in HDAC1-mediated transcriptional repression". Proceedings of the National Academy of Sciences of the United States of America 95 (7): 3519–3524. March 1998. doi:10.1073/pnas.95.7.3519. PMID 9520398. Bibcode: 1998PNAS...95.3519H.
- ↑ 39.0 39.1 39.2 "Histone deacetylases and SAP18, a novel polypeptide, are components of a human Sin3 complex". Cell 89 (3): 357–364. May 1997. doi:10.1016/s0092-8674(00)80216-0. PMID 9150135.
- ↑ "TGIF2 interacts with histone deacetylase 1 and represses transcription". The Journal of Biological Chemistry 276 (34): 32109–32114. August 2001. doi:10.1074/jbc.M103377200. PMID 11427533.
- ↑ "Human Sin3 deacetylase and trithorax-related Set1/Ash2 histone H3-K4 methyltransferase are tethered together selectively by the cell-proliferation factor HCF-1". Genes & Development 17 (7): 896–911. April 2003. doi:10.1101/gad.252103. PMID 12670868.
- ↑ "TIS7 interacts with the mammalian SIN3 histone deacetylase complex in epithelial cells". The EMBO Journal 21 (17): 4621–4631. September 2002. doi:10.1093/emboj/cdf461. PMID 12198164.
- ↑ 43.0 43.1 "Repression by Ikaros and Aiolos is mediated through histone deacetylase complexes". The EMBO Journal 18 (11): 3090–3100. June 1999. doi:10.1093/emboj/18.11.3090. PMID 10357820.
- ↑ "A molecular dissection of the repression circuitry of Ikaros". The Journal of Biological Chemistry 277 (31): 27697–27705. August 2002. doi:10.1074/jbc.M201694200. PMID 12015313.
- ↑ "Human ING1 proteins differentially regulate histone acetylation". The Journal of Biological Chemistry 277 (33): 29832–29839. August 2002. doi:10.1074/jbc.M200197200. PMID 12015309.
- ↑ "MBD3 and HDAC1, two components of the NuRD complex, are localized at Aurora-A-positive centrosomes in M phase". The Journal of Biological Chemistry 277 (50): 48714–48723. December 2002. doi:10.1074/jbc.M208461200. PMID 12354758.
- ↑ "The mCpG-binding domain of human MBD3 does not bind to mCpG but interacts with NuRD/Mi2 components HDAC1 and MTA2". The Journal of Biological Chemistry 277 (38): 35434–35439. September 2002. doi:10.1074/jbc.M203455200. PMID 12124384.
- ↑ "Human MI-ER1 alpha and beta function as transcriptional repressors by recruitment of histone deacetylase 1 to their conserved ELM2 domain". Molecular and Cellular Biology 23 (1): 250–258. January 2003. doi:10.1128/mcb.23.1.250-258.2003. PMID 12482978.
- ↑ "MLL repression domain interacts with histone deacetylases, the polycomb group proteins HPC2 and BMI-1, and the corepressor C-terminal-binding protein". Proceedings of the National Academy of Sciences of the United States of America 100 (14): 8342–8347. July 2003. doi:10.1073/pnas.1436338100. PMID 12829790. Bibcode: 2003PNAS..100.8342X.
- ↑ "Transcriptional repression of oestrogen receptor by metastasis-associated protein 1 corepressor". Nature Cell Biology 3 (1): 30–37. January 2001. doi:10.1038/35050532. PMID 11146623.
- ↑ 51.0 51.1 51.2 51.3 "CoREST is an integral component of the CoREST- human histone deacetylase complex". Proceedings of the National Academy of Sciences of the United States of America 98 (4): 1454–1458. February 2001. doi:10.1073/pnas.98.4.1454. PMID 11171972. Bibcode: 2001PNAS...98.1454Y.
- ↑ 52.0 52.1 52.2 "SATB1 targets chromatin remodelling to regulate genes over long distances". Nature 419 (6907): 641–645. October 2002. doi:10.1038/nature01084. PMID 12374985. Bibcode: 2002Natur.419..641Y. https://digital.library.unt.edu/ark:/67531/metadc733622/.
- ↑ "MDM2-HDAC1-mediated deacetylation of p53 is required for its degradation". The EMBO Journal 21 (22): 6236–6245. November 2002. doi:10.1093/emboj/cdf616. PMID 12426395.
- ↑ 54.0 54.1 54.2 "MBD2 is a transcriptional repressor belonging to the MeCP1 histone deacetylase complex". Nature Genetics 23 (1): 58–61. September 1999. doi:10.1038/12659. PMID 10471499.
- ↑ "Two highly related p66 proteins comprise a new family of potent transcriptional repressors interacting with MBD2 and MBD3". The Journal of Biological Chemistry 277 (43): 40958–40966. October 2002. doi:10.1074/jbc.M207467200. PMID 12183469.
- ↑ "A Smad transcriptional corepressor". Cell 97 (1): 29–39. April 1999. doi:10.1016/s0092-8674(00)80712-6. PMID 10199400.
- ↑ 57.0 57.1 "A MyoD-dependent differentiation checkpoint: ensuring genome integrity". Developmental Cell 3 (6): 757–758. December 2002. doi:10.1016/s1534-5807(02)00372-6. PMID 12479798.
- ↑ "A role for histone deacetylase HDAC1 in modulating the transcriptional activity of MyoD: inhibition of the myogenic program". The EMBO Journal 20 (7): 1739–1753. April 2001. doi:10.1093/emboj/20.7.1739. PMID 11285237.
- ↑ 59.0 59.1 "The phosphorylation status of nuclear NF-kappa B determines its association with CBP/p300 or HDAC-1". Molecular Cell 9 (3): 625–636. March 2002. doi:10.1016/s1097-2765(02)00477-x. PMID 11931769.
- ↑ "A novel nuclear receptor corepressor complex, N-CoR, contains components of the mammalian SWI/SNF complex and the corepressor KAP-1". The Journal of Biological Chemistry 275 (51): 40463–40470. December 2000. doi:10.1074/jbc.M007864200. PMID 11013263.
- ↑ "Histone deacetylase 1 expression is inversely correlated with age in the short-lived fish Nothobranchius furzeri". Histochemistry and Cell Biology 150 (3): 255–269. 28 June 2018. doi:10.1007/s00418-018-1687-4. PMID 29951776.
- ↑ "Proliferating cell nuclear antigen associates with histone deacetylase activity, integrating DNA replication and chromatin modification". The Journal of Biological Chemistry 277 (23): 20974–20978. June 2002. doi:10.1074/jbc.M202504200. PMID 11929879.
- ↑ "Characterization of BHC80 in BRAF-HDAC complex, involved in neuron-specific gene repression". Biochemical and Biophysical Research Communications 322 (2): 601–608. September 2004. doi:10.1016/j.bbrc.2004.07.163. PMID 15325272. Bibcode: 2004BBRC..322..601I.
- ↑ "A putative coiled-coil domain of prohibitin is sufficient to repress E2F1-mediated transcription and induce apoptosis". Biochemical and Biophysical Research Communications 312 (2): 459–466. December 2003. doi:10.1016/j.bbrc.2003.10.148. PMID 14637159. Bibcode: 2003BBRC..312..459J.
- ↑ 65.0 65.1 "Prohibitin co-localizes with Rb in the nucleus and recruits N-CoR and HDAC1 for transcriptional repression". Oncogene 21 (55): 8388–8396. December 2002. doi:10.1038/sj.onc.1205944. PMID 12466959.
- ↑ "Role of PML and PML-RARalpha in Mad-mediated transcriptional repression". Molecular Cell 7 (6): 1233–1243. June 2001. doi:10.1016/s1097-2765(01)00257-x. PMID 11430826.
- ↑ "The growth suppressor PML represses transcription by functionally and physically interacting with histone deacetylases". Molecular and Cellular Biology 21 (7): 2259–2268. April 2001. doi:10.1128/MCB.21.7.2259-2268.2001. PMID 11259576.
- ↑ 68.0 68.1 "Dual mechanisms of regulation of transcription of luteinizing hormone receptor gene by nuclear orphan receptors and histone deacetylase complexes". The Journal of Steroid Biochemistry and Molecular Biology 85 (2–5): 401–414. June 2003. doi:10.1016/s0960-0760(03)00230-9. PMID 12943729. https://zenodo.org/record/1260176.
- ↑ 69.0 69.1 69.2 "Silencing of transcription of the human luteinizing hormone receptor gene by histone deacetylase-mSin3A complex". The Journal of Biological Chemistry 277 (36): 33431–33438. September 2002. doi:10.1074/jbc.M204417200. PMID 12091390.
- ↑ "The histone deacetylase HDAC3 targets RbAp48 to the retinoblastoma protein". Nucleic Acids Research 29 (15): 3131–3136. August 2001. doi:10.1093/nar/29.15.3131. PMID 11470869.
- ↑ "Histone deacetylase activity is required for full transcriptional repression by mSin3A". Cell 89 (3): 341–347. May 1997. doi:10.1016/s0092-8674(00)80214-7. PMID 9150133.
- ↑ "Post-activation turn-off of NF-kappa B-dependent transcription is regulated by acetylation of p65". The Journal of Biological Chemistry 278 (4): 2758–2766. January 2003. doi:10.1074/jbc.M209572200. PMID 12419806.
- ↑ "The large subunit of replication factor C interacts with the histone deacetylase, HDAC1". The Journal of Biological Chemistry 277 (33): 29550–29554. August 2002. doi:10.1074/jbc.M200513200. PMID 12045192.
- ↑ 74.0 74.1 74.2 "The three members of the pocket proteins family share the ability to repress E2F activity through recruitment of a histone deacetylase". Proceedings of the National Academy of Sciences of the United States of America 95 (18): 10493–10498. September 1998. doi:10.1073/pnas.95.18.10493. PMID 9724731. Bibcode: 1998PNAS...9510493F.
- ↑ 75.0 75.1 "RBP1 recruits both histone deacetylase-dependent and -independent repression activities to retinoblastoma family proteins". Molecular and Cellular Biology 19 (10): 6632–6641. October 1999. doi:10.1128/mcb.19.10.6632. PMID 10490602.
- ↑ "Mutagenesis of the pRB pocket reveals that cell cycle arrest functions are separable from binding to viral oncoproteins". Molecular and Cellular Biology 20 (10): 3715–3727. May 2000. doi:10.1128/mcb.20.10.3715-3727.2000. PMID 10779361.
- ↑ "DNA methyltransferase Dnmt1 associates with histone deacetylase activity". Nature Genetics 24 (1): 88–91. January 2000. doi:10.1038/71750. PMID 10615135.
- ↑ "Rb interacts with histone deacetylase to repress transcription". Cell 92 (4): 463–473. February 1998. doi:10.1016/s0092-8674(00)80940-x. PMID 9491888.
- ↑ "Transforming growth factor-beta1 recruits histone deacetylase 1 to a p130 repressor complex in transgenic mice in vivo". Cancer Research 60 (16): 4531–4537. August 2000. PMID 10969803.
- ↑ "Modulation of YY1 activity by SAP30". Biochemical and Biophysical Research Communications 306 (1): 267–275. June 2003. doi:10.1016/S0006-291X(03)00966-5. PMID 12788099. Bibcode: 2003BBRC..306..267H.
- ↑ "SAP30, a novel protein conserved between human and yeast, is a component of a histone deacetylase complex". Molecular Cell 1 (7): 1021–1031. June 1998. doi:10.1016/s1097-2765(00)80102-1. PMID 9651585.
- ↑ "HBP1 and Mad1 repressors bind the Sin3 corepressor PAH2 domain with opposite helical orientations". Nature Structural & Molecular Biology 11 (8): 738–746. August 2004. doi:10.1038/nsmb798. PMID 15235594.
- ↑ "Pf1, a novel PHD zinc finger protein that links the TLE corepressor to the mSin3A-histone deacetylase complex". Molecular and Cellular Biology 21 (13): 4110–4118. July 2001. doi:10.1128/MCB.21.13.4110-4118.2001. PMID 11390640.
- ↑ 84.0 84.1 "Identification and characterization of three new components of the mSin3A corepressor complex". Molecular and Cellular Biology 23 (10): 3456–3467. May 2003. doi:10.1128/mcb.23.10.3456-3467.2003. PMID 12724404.
- ↑ "An ERG (ets-related gene)-associated histone methyltransferase interacts with histone deacetylases 1/2 and transcription co-repressors mSin3A/B". The Biochemical Journal 369 (Pt 3): 651–657. February 2003. doi:10.1042/BJ20020854. PMID 12398767.
- ↑ "The N-CoR-HDAC3 nuclear receptor corepressor complex inhibits the JNK pathway through the integral subunit GPS2". Molecular Cell 9 (3): 611–623. March 2002. doi:10.1016/s1097-2765(02)00468-9. PMID 11931768.
- ↑ "Nuclear receptor corepressors partner with class II histone deacetylases in a Sin3-independent repression pathway". Genes & Development 14 (1): 45–54. January 2000. doi:10.1101/gad.14.1.45. PMID 10640275.
- ↑ "Sharp, an inducible cofactor that integrates nuclear receptor repression and activation". Genes & Development 15 (9): 1140–1151. May 2001. doi:10.1101/gad.871201. PMID 11331609.
- ↑ "Identification of mammalian Sds3 as an integral component of the Sin3/histone deacetylase corepressor complex". Molecular and Cellular Biology 22 (8): 2743–2750. April 2002. doi:10.1128/mcb.22.8.2743-2750.2002. PMID 11909966.
- ↑ "Functional and physical interaction between the histone methyl transferase Suv39H1 and histone deacetylases". Nucleic Acids Research 30 (2): 475–481. January 2002. doi:10.1093/nar/30.2.475. PMID 11788710.
- ↑ "Che-1 arrests human colon carcinoma cell proliferation by displacing HDAC1 from the p21WAF1/CIP1 promoter". The Journal of Biological Chemistry 278 (38): 36496–36504. September 2003. doi:10.1074/jbc.M306694200. PMID 12847090.
- ↑ "Constitutive expression of the Id-1 promoter in human metastatic breast cancer cells is linked with the loss of NF-1/Rb/HDAC-1 transcription repressor complex". Oncogene 21 (12): 1812–1822. March 2002. doi:10.1038/sj.onc.1205252. PMID 11896613.
- ↑ "The transcriptional repressor Sp3 is associated with CK2-phosphorylated histone deacetylase 2". The Journal of Biological Chemistry 277 (39): 35783–35786. September 2002. doi:10.1074/jbc.C200378200. PMID 12176973.
- ↑ 94.0 94.1 "Histone deacetylase interacts directly with DNA topoisomerase II". Nature Genetics 26 (3): 349–353. November 2000. doi:10.1038/81671. PMID 11062478.
- ↑ 95.0 95.1 "Deacetylase activity associates with topoisomerase II and is necessary for etoposide-induced apoptosis". The Journal of Biological Chemistry 276 (7): 4539–4542. February 2001. doi:10.1074/jbc.C000824200. PMID 11136718.
- ↑ "HDAC4 mediates transcriptional repression by the acute promyelocytic leukaemia-associated protein PLZF". Oncogene 23 (54): 8777–8784. November 2004. doi:10.1038/sj.onc.1208128. PMID 15467736.
- ↑ "Components of the SMRT corepressor complex exhibit distinctive interactions with the POZ domain oncoproteins PLZF, PLZF-RARalpha, and BCL-6". The Journal of Biological Chemistry 273 (42): 27695–27702. October 1998. doi:10.1074/jbc.273.42.27695. PMID 9765306.
Further reading
- "Histone deacetylase: a regulator of transcription". Science (New York, N.Y.) 272 (5260): 371–372. April 1996. doi:10.1126/science.272.5260.371. PMID 8602525. Bibcode: 1996Sci...272..371W. https://zenodo.org/record/1231070.
- "NuRD and SIN3 histone deacetylase complexes in development". Trends in Genetics 16 (8): 351–356. August 2000. doi:10.1016/S0168-9525(00)02066-7. PMID 10904264.
- "Class II histone deacetylases: versatile regulators". Trends in Genetics 19 (5): 286–293. May 2003. doi:10.1016/S0168-9525(03)00073-8. PMID 12711221.
- "Dual mechanisms of regulation of transcription of luteinizing hormone receptor gene by nuclear orphan receptors and histone deacetylase complexes". The Journal of Steroid Biochemistry and Molecular Biology 85 (2–5): 401–414. June 2003. doi:10.1016/S0960-0760(03)00230-9. PMID 12943729. https://zenodo.org/record/1260176.
- "The regulation of HIV-1 transcription: molecular targets for chemotherapeutic intervention". Medicinal Research Reviews 26 (5): 595–625. September 2006. doi:10.1002/med.20081. PMID 16838299.
- "E2F-5, a new E2F family member that interacts with p130 in vivo". Molecular and Cellular Biology 15 (6): 3082–3089. June 1995. doi:10.1128/mcb.15.6.3082. PMID 7760804.
- "Oligo-capping: a simple method to replace the cap structure of eukaryotic mRNAs with oligoribonucleotides". Gene 138 (1–2): 171–174. January 1994. doi:10.1016/0378-1119(94)90802-8. PMID 8125298.
- "Human transcription factor YY1 represses human immunodeficiency virus type 1 transcription and virion production". Journal of Virology 68 (2): 905–910. February 1994. doi:10.1128/JVI.68.2.905-910.1994. PMID 8289393.
- "Isolation and mapping of a human gene (RPD3L1) that is homologous to RPD3, a transcription factor in Saccharomyces cerevisiae". Cytogenetics and Cell Genetics 73 (1–2): 130–133. 1996. doi:10.1159/000134323. PMID 8646880.
- "Histone deacetylase activity is required for full transcriptional repression by mSin3A". Cell 89 (3): 341–347. May 1997. doi:10.1016/S0092-8674(00)80214-7. PMID 9150133.
- "Histone deacetylases associated with the mSin3 corepressor mediate mad transcriptional repression". Cell 89 (3): 349–356. May 1997. doi:10.1016/S0092-8674(00)80215-9. PMID 9150134.
- "Histone deacetylases and SAP18, a novel polypeptide, are components of a human Sin3 complex". Cell 89 (3): 357–364. May 1997. doi:10.1016/S0092-8674(00)80216-0. PMID 9150135.
- "Repression of human immunodeficiency virus type 1 through the novel cooperation of human factors YY1 and LSF". Journal of Virology 71 (12): 9375–9382. December 1997. doi:10.1128/JVI.71.12.9375-9382.1997. PMID 9371597.
- "Construction and characterization of a full length-enriched and a 5'-end-enriched cDNA library". Gene 200 (1–2): 149–156. October 1997. doi:10.1016/S0378-1119(97)00411-3. PMID 9373149.
- "Retinoblastoma protein recruits histone deacetylase to repress transcription". Nature 391 (6667): 597–601. February 1998. doi:10.1038/35404. PMID 9468139. Bibcode: 1998Natur.391..597B.
- "Retinoblastoma protein represses transcription by recruiting a histone deacetylase". Nature 391 (6667): 601–605. February 1998. doi:10.1038/35410. PMID 9468140. Bibcode: 1998Natur.391..601M.
- "Role of the histone deacetylase complex in acute promyelocytic leukaemia". Nature 391 (6669): 811–814. February 1998. doi:10.1038/35895. PMID 9486654. Bibcode: 1998Natur.391..811L.
- "Rb interacts with histone deacetylase to repress transcription". Cell 92 (4): 463–473. February 1998. doi:10.1016/S0092-8674(00)80940-X. PMID 9491888.
External links
- HDAC1+protein,+human at the US National Library of Medicine Medical Subject Headings (MeSH)
 |  |
