Wikipedia

HDAC1

Histon-deacetilaza 1 (HDAC1) jest enzim koji je kod ljudi kodiran genom HDAC1 sa hromosoma 1.[5]

HDAC1
Dostupne strukture
PDBPretraga ortologa: PDBe RCSB
Spisak PDB ID kodova

4BKX, 5ICN

Identifikatori
AliasiHDAC1
Vanjski ID-jeviOMIM: 601241 MGI: 108086 HomoloGene: 68426 GeneCards: HDAC1
Lokacija gena (čovjek)
Hromosom 1 (čovjek)
Hrom.Hromosom 1 (čovjek)[1]
Hromosom 1 (čovjek)
Genomska lokacija za HDAC1
Genomska lokacija za HDAC1
Bend1p35.2-p35.1Početak32,292,083 bp[1]
Kraj32,333,635 bp[1]
Lokacija gena (miš)
Hromosom 4 (miš)
Hrom.Hromosom 4 (miš)[2]
Hromosom 4 (miš)
Genomska lokacija za HDAC1
Genomska lokacija za HDAC1
Bend4 D2.2|4 63.26 cMPočetak129,409,897 bp[2]
Kraj129,436,506 bp[2]
Obrazac RNK ekspresije
Više referentnih podataka o ekspresiji
Ontologija gena
Molekularna funkcija• GO:0000980 RNA polymerase II cis-regulatory region sequence-specific DNA binding
• NAD-dependent histone deacetylase activity (H3-K14 specific)
• GO:0001106 transcription corepressor activity
• histone deacetylase activity
• protein N-terminus binding
• GO:0001131, GO:0001151, GO:0001130, GO:0001204 DNA-binding transcription factor activity
• protein deacetylase activity
• histone deacetylase binding
• GO:0000975 transcription cis-regulatory region binding
• NF-kappaB binding
• deacetylase activity
• GO:0001948, GO:0016582 vezivanje za proteine
• nucleosomal DNA binding
• vezivanje enzima
• hydrolase activity
• core promoter sequence-specific DNA binding
• p53 binding
• transcription factor binding
• RNA polymerase II core promoter sequence-specific DNA binding
• vezivanje sa DNK
• chromatin binding
• Krueppel-associated box domain binding
• E-box binding
• promoter-specific chromatin binding
Ćelijska komponenta• citoplazma
• NuRD complex
• citosol
• histone deacetylase complex
• Sin3 complex
• nukleoplazma
• jedro
• Hromatin
• GO:0035328 heterochromatin
• transcription regulator complex
• transcription repressor complex
• GO:0009327 makromolekulani kompleks
• soma
• Sin3-type complex
Biološki proces• hair follicle placode formation
• epidermal cell differentiation
• chromatin remodeling
• GO:0009373 regulation of transcription, DNA-templated
• rhythmic process
• negative regulation of androgen receptor signaling pathway
• embryonic digit morphogenesis
• negative regulation of apoptotic process
• Koagulacija (krv)
• GO:1901227 negative regulation of transcription by RNA polymerase II
• eyelid development in camera-type eye
• circadian regulation of gene expression
• negative regulation of gene expression
• GO:0060469, GO:0009371 positive regulation of transcription, DNA-templated
• odontogenesis of dentin-containing tooth
• protein deacetylation
• histone H4 deacetylation
• fungiform papilla formation
• negative regulation of myotube differentiation
• GO:0022415 viral process
• histone deacetylation
• negative regulation of canonical Wnt signaling pathway
• GO:0003257, GO:0010735, GO:1901228, GO:1900622, GO:1904488 positive regulation of transcription by RNA polymerase II
• transcription, DNA-templated
• regulation of signal transduction by p53 class mediator
• DNA methylation-dependent heterochromatin assembly
• beta-catenin-TCF complex assembly
• GO:0031497, GO:0006336, GO:0034724, GO:0001301, GO:0007580, GO:0034652, GO:0010847 chromatin organization
• positive regulation of cell population proliferation
• GO:0045996 negative regulation of transcription, DNA-templated
• histone H3 deacetylation
• regulation of megakaryocyte differentiation
• GO:0044324, GO:0003256, GO:1901213, GO:0046019, GO:0046020, GO:1900094, GO:0061216, GO:0060994, GO:1902064, GO:0003258, GO:0072212 regulation of transcription by RNA polymerase II
• endoderm development
• Jednodnevni biološki ritam
• hippocampus development
• neuron differentiation
• negative regulation of I-kappaB kinase/NF-kappaB signaling
• positive regulation of oligodendrocyte differentiation
• regulation of endopeptidase activity
• regulation of amyloid-beta clearance
• negative regulation of intrinsic apoptotic signaling pathway
Izvori:Amigo / QuickGO
Ortolozi
VrsteČovjekMiš
Entrez

3065

433759

Ensembl

ENSG00000116478

ENSMUSG00000028800

UniProt

Q13547

O09106

RefSeq (mRNK)

NM_004964

NM_008228

RefSeq (bjelančevina)

NP_004955

NP_032254

Lokacija (UCSC)Chr 1: 32.29 – 32.33 MbChr 4: 129.41 – 129.44 Mb
PubMed pretraga[3][4]
Wikipodaci
Pogledaj/uredi – čovjekPogledaj/uredi – miš

Aminokiselinska sekvenca

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Dužina polipeptidnog lanca je 482 aminokiseline, a molekulska težina Da. 55.103[6]

1020304050
MAQTQGTRRKVCYYYDGDVGNYYYGQGHPMKPHRIRMTHNLLLNYGLYRK
MEIYRPHKANAEEMTKYHSDDYIKFLRSIRPDNMSEYSKQMQRFNVGEDC
PVFDGLFEFCQLSTGGSVASAVKLNKQQTDIAVNWAGGLHHAKKSEASGF
CYVNDIVLAILELLKYHQRVLYIDIDIHHGDGVEEAFYTTDRVMTVSFHK
YGEYFPGTGDLRDIGAGKGKYYAVNYPLRDGIDDESYEAIFKPVMSKVME
MFQPSAVVLQCGSDSLSGDRLGCFNLTIKGHAKCVEFVKSFNLPMLMLGG
GGYTIRNVARCWTYETAVALDTEIPNELPYNDYFEYFGPDFKLHISPSNM
TNQNTNEYLEKIKQRLFENLRMLPHAPGVQMQAIPEDAIPEESGDEDEDD
PDKRISICSSDKRIACEEEFSDSEEEGEGGRKNSSNFKKAKRVKTEDEKE
KDPEEKKEVTEEEKTKEEKPEAKGVKEEVKLA

4

Funkcija

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Acetilacija i deacetilacija histona, katalizirana kompleksima više podjedinica, ima ključnu ulogu u regulaciji eukariotske ekspresije gena. Protein kodiran ovim genom pripada porodici histon deacetilaza/acuc/alfa i komponenta je kompleksa histon-deacetilaza. Također je u interakciji sa proteinom supresorom tumora retinoblastoma i ovaj kompleks je ključni element u kontroli proliferacije i diferencijacije ćelija. Zajedno s proteinom-2 MTA2 povezanim s metastazama, deacetilira p53 i modulira njegov učinak na rast i ćelijsku apoptozu.[7]

Modelni organizmi

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Fenotip Hdac1 nokaut-miševa
Svojstvo Fenotip
Vijabilnost homozigot Nenormalan
Studija recesivne letalnosti Nenormalan
Plodnost Normalan
Tjelesna težina Normalan
Anksioznost otvorenog polja Normalan
Neurološka procjena Normalan
Snaga stiska Normalan
Test vruće ploče Normalan
Dismorfologija Normalan
Indirektna kalorimetrija Normalan
Test tolerancije glukoze Normalan
Slušni odgovor moždanog stabla Normalan
DEXA Normalan
Radiografija Normalan
Tjelesna temperatura Normalan
Morfologija oka Normalan
Klinička hemija Normalan
Hematologija Normalan
Limfociti periferne krvi Normalan
Mikronukleus test Normalan
Težina srca Normalan
Histopatologija mozga Normalan
Histopatologija oka Normalan
Salmonella infekcija Normalan[8]
Citrobacter infekcija Normalan[9]
Svi testovi i analize prema[10][11]

U proučavanju funkcije HDAC1 korišteni su modelni organizmi. Uvjetna linija nokaut-miševa, zvana Hdac1tm1a(EUCOMM)Wtsi[12][13] gwnwrirana je kao dio programa Međunarodnog konzorcija za nokaut-miševe — visokoprolpusnog projekta mutageneze za generiranje i distribuciju modela životzinjskih bolesti zainteresiranim naučnicima — na Institutu Wellcome Trust Sanger.[14][15][16] Mužjaci i ženke podvrgnute su standardiziranom fenotipskom pregledu kako bi se utvrdili efekti delecija.[10][17] Obavljeno je 25 testova i prijavljena su dva nenormalna fenotipa. Tokom gestacije identifikovan je smanjen broj homozigotnih mutantnih embriona, a nijedan nije preživio do odbijanja. Preostali testovi su obavljeni na heterozigot nimmutantnim odraslim miševima i kod ovih životinja nisu uočene značajne abnormalnosti.[10]

Interakcije

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Pokazalo se da HDAC1 interraguje sa:

Također pogledajte

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Reference

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  1. ^ a b c GRCh38: Ensembl release 89: ENSG00000116478 - Ensembl, maj 2017
  2. ^ a b c GRCm38: Ensembl release 89: ENSMUSG00000028800 - Ensembl, maj 2017
  3. ^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  4. ^ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  5. ^ Taunton J, Hassig CA, Schreiber SL (april 1996). "A mammalian histone deacetylase related to the yeast transcriptional regulator Rpd3p". Science. 272 (5260): 408–11. Bibcode:1996Sci...272..408T. doi:10.1126/science.272.5260.408. PMID 8602529. S2CID 25717734.
  6. ^ "UniProt, Q13547" (jezik: eng.). Pristupljeno 28. 11. 2021.CS1 održavanje: nepoznati jezik (link)
  7. ^ "Entrez Gene: HDAC1 histone deacetylase 1".
  8. ^ "Salmonella infection data for Hdac1". Wellcome Trust Sanger Institute.
  9. ^ "Citrobacter infection data for Hdac1". Wellcome Trust Sanger Institute.
  10. ^ a b c Gerdin AK (2010). "The Sanger Mouse Genetics Programme: High throughput characterisation of knockout mice". Acta Ophthalmologica. 88 (S248). doi:10.1111/j.1755-3768.2010.4142.x. S2CID 85911512.
  11. ^ Mouse Resources Portal, Wellcome Trust Sanger Institute.
  12. ^ "International Knockout Mouse Consortium". Arhivirano s originala, 20. 3. 2012. Pristupljeno 5. 1. 2012.
  13. ^ "Mouse Genome Informatics".
  14. ^ Skarnes WC, Rosen B, West AP, Koutsourakis M, Bushell W, Iyer V, Mujica AO, Thomas M, Harrow J, Cox T, Jackson D, Severin J, Biggs P, Fu J, Nefedov M, de Jong PJ, Stewart AF, Bradley A (juni 2011). "A conditional knockout resource for the genome-wide study of mouse gene function". Nature. 474 (7351): 337–42. doi:10.1038/nature10163. PMC 3572410. PMID 21677750.
  15. ^ Dolgin E (juni 2011). "Mouse library set to be knockout". Nature. 474 (7351): 262–3. doi:10.1038/474262a. PMID 21677718.
  16. ^ Collins FS, Rossant J, Wurst W (januar 2007). "A mouse for all reasons". Cell. 128 (1): 9–13. doi:10.1016/j.cell.2006.12.018. PMID 17218247. S2CID 18872015.
  17. ^ van der Weyden L, White JK, Adams DJ, Logan DW (juni 2011). "The mouse genetics toolkit: revealing function and mechanism". Genome Biology. 12 (6): 224. doi:10.1186/gb-2011-12-6-224. PMC 3218837. PMID 21722353.
  18. ^ Gaughan L, Logan IR, Cook S, Neal DE, Robson CN (juli 2002). "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): 25904–13. doi:10.1074/jbc.M203423200. PMID 11994312.
  19. ^ a b David G, Alland L, Hong SH, Wong CW, DePinho RA, Dejean A (maj 1998). "Histone deacetylase associated with mSin3A mediates repression by the acute promyelocytic leukemia-associated PLZF protein". Oncogene. 16 (19): 2549–56. doi:10.1038/sj.onc.1202043. PMID 9627120.
  20. ^ Deltour S, Guerardel C, Leprince D (decembar 1999). "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): 14831–6. Bibcode:1999PNAS...9614831D. doi:10.1073/pnas.96.26.14831. PMC 24733. PMID 10611298.
  21. ^ Farioli-Vecchioli S, Tanori M, Micheli L, Mancuso M, Leonardi L, Saran A, Ciotti MT, Ferretti E, Gulino A, Pazzaglia S, Tirone F (juli 2007). "Inhibition of medulloblastoma tumorigenesis by the antiproliferative and pro-differentiative gene PC3". FASEB Journal. 21 (9): 2215–25. doi:10.1096/fj.06-7548com. PMID 17371797. S2CID 4974360.
  22. ^ Micheli L, D'Andrea G, Leonardi L, Tirone F (juli 2017). "HDAC1, HDAC4, and HDAC9 Bind to PC3/Tis21/Btg2 and Are Required for Its Inhibition of Cell Cycle Progression and Cyclin D1 Expression" (PDF). Journal of Cellular Physiology. 232 (7): 1696–1707. doi:10.1002/jcp.25467. PMID 27333946. S2CID 4070837.
  23. ^ a b c d e f Yoon YM, Baek KH, Jeong SJ, Shin HJ, Ha GH, Jeon AH, Hwang SG, Chun JS, Lee CW (septembar 2004). "WD repeat-containing mitotic checkpoint proteins act as transcriptional repressors during interphase". FEBS Letters. 575 (1–3): 23–9. doi:10.1016/j.febslet.2004.07.089. PMID 15388328. S2CID 21762011.
  24. ^ Hoogeveen AT, Rossetti S, Stoyanova V, Schonkeren J, Fenaroli A, Schiaffonati L, van Unen L, Sacchi N (septembar 2002). "The transcriptional corepressor MTG16a contains a novel nucleolar targeting sequence deranged in t (16; 21)-positive myeloid malignancies". Oncogene. 21 (43): 6703–12. doi:10.1038/sj.onc.1205882. PMID 12242670.
  25. ^ Amann JM, Nip J, Strom DK, Lutterbach B, Harada H, Lenny N, Downing JR, Meyers S, Hiebert SW (oktobar 2001). "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): 6470–83. doi:10.1128/mcb.21.19.6470-6483.2001. PMC 99794. PMID 11533236.
  26. ^ a b c d Tong JK, Hassig CA, Schnitzler GR, Kingston RE, Schreiber SL (oktobar 1998). "Chromatin deacetylation by an ATP-dependent nucleosome remodelling complex". Nature. 395 (6705): 917–21. Bibcode:1998Natur.395..917T. doi:10.1038/27699. PMID 9804427. S2CID 4355885.
  27. ^ a b c d Kuzmichev A, Zhang Y, Erdjument-Bromage H, Tempst P, Reinberg D (februar 2002). "Role of the Sin3-histone deacetylase complex in growth regulation by the candidate tumor suppressor p33(ING1)". Molecular and Cellular Biology. 22 (3): 835–48. doi:10.1128/mcb.22.3.835-848.2002. PMC 133546. PMID 11784859.
  28. ^ a b c d e f g Yao YL, Yang WM (oktobar 2003). "The metastasis-associated proteins 1 and 2 form distinct protein complexes with histone deacetylase activity". The Journal of Biological Chemistry. 278 (43): 42560–8. doi:10.1074/jbc.M302955200. PMID 12920132.
  29. ^ a b c Grozinger CM, Hassig CA, Schreiber SL (april 1999). "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): 4868–73. Bibcode:1999PNAS...96.4868G. doi:10.1073/pnas.96.9.4868. PMC 21783. PMID 10220385.
  30. ^ Smirnov DA, Hou S, Ricciardi RP (mart 2000). "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): 319–28. doi:10.1006/viro.1999.0181. PMID 10704340.
  31. ^ a b Melhuish TA, Wotton D (decembar 2000). "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): 39762–6. doi:10.1074/jbc.C000416200. PMID 10995736.
  32. ^ Zhang CL, McKinsey TA, Lu JR, Olson EN (januar 2001). "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): 35–9. doi:10.1074/jbc.M007364200. PMID 11022042.
  33. ^ Sundqvist A, Sollerbrant K, Svensson C (juni 1998). "The carboxy-terminal region of adenovirus E1A activates transcription through targeting of a C-terminal binding protein-histone deacetylase complex". FEBS Letters. 429 (2): 183–8. doi:10.1016/s0014-5793(98)00588-2. PMID 9650586.
  34. ^ a b Wilson BJ, Bates GJ, Nicol SM, Gregory DJ, Perkins ND, Fuller-Pace FV (august 2004). "The p68 and p72 DEAD box RNA helicases interact with HDAC1 and repress transcription in a promoter-specific manner". BMC Molecular Biology. 5: 11. doi:10.1186/1471-2199-5-11. PMC 514542. PMID 15298701.
  35. ^ Fuks F, Burgers WA, Godin N, Kasai M, Kouzarides T (maj 2001). "Dnmt3a binds deacetylases and is recruited by a sequence-specific repressor to silence transcription". The EMBO Journal. 20 (10): 2536–44. doi:10.1093/emboj/20.10.2536. PMC 125250. PMID 11350943.
  36. ^ Aapola U, Liiv I, Peterson P (august 2002). "Imprinting regulator DNMT3L is a transcriptional repressor associated with histone deacetylase activity". Nucleic Acids Research. 30 (16): 3602–8. doi:10.1093/nar/gkf474. PMC 134241. PMID 12177302.
  37. ^ Deplus R, Brenner C, Burgers WA, Putmans P, Kouzarides T, de Launoit Y, Fuks F (septembar 2002). "Dnmt3L is a transcriptional repressor that recruits histone deacetylase". Nucleic Acids Research. 30 (17): 3831–8. doi:10.1093/nar/gkf509. PMC 137431. PMID 12202768.
  38. ^ Li H, Leo C, Zhu J, Wu X, O'Neil J, Park EJ, Chen JD (mart 2000). "Sequestration and inhibition of Daxx-mediated transcriptional repression by PML". Molecular and Cellular Biology. 20 (5): 1784–96. doi:10.1128/mcb.20.5.1784-1796.2000. PMC 85360. PMID 10669754.
  39. ^ a b c van der Vlag J, Otte AP (decembar 1999). "Transcriptional repression mediated by the human polycomb-group protein EED involves histone deacetylation". Nature Genetics. 23 (4): 474–8. doi:10.1038/70602. PMID 10581039. S2CID 6748531.
  40. ^ Vinatzer U, Taplick J, Seiser C, Fonatsch C, Wieser R (septembar 2001). "The leukaemia-associated transcription factors EVI-1 and MDS1/EVI1 repress transcription and interact with histone deacetylase". British Journal of Haematology. 114 (3): 566–73. doi:10.1046/j.1365-2141.2001.02987.x. PMID 11552981.
  41. ^ Chakraborty S, Senyuk V, Sitailo S, Chi Y, Nucifora G (novembar 2001). "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): 44936–43. doi:10.1074/jbc.M106733200. PMID 11568182.
  42. ^ Yang WM, Yao YL, Seto E (septembar 2001). "The FK506-binding protein 25 functionally associates with histone deacetylases and with transcription factor YY1". The EMBO Journal. 20 (17): 4814–25. doi:10.1093/emboj/20.17.4814. PMC 125595. PMID 11532945.
  43. ^ Watamoto K, Towatari M, Ozawa Y, Miyata Y, Okamoto M, Abe A, Naoe T, Saito H (decembar 2003). "Altered interaction of HDAC5 with GATA-1 during MEL cell differentiation". Oncogene. 22 (57): 9176–84. doi:10.1038/sj.onc.1206902. PMID 14668799.
  44. ^ a b c d Hakimi MA, Bochar DA, Chenoweth J, Lane WS, Mandel G, Shiekhattar R (maj 2002). "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): 7420–5. Bibcode:2002PNAS...99.7420H. doi:10.1073/pnas.112008599. PMC 124246. PMID 12032298.
  45. ^ a b Johnson CA, White DA, Lavender JS, O'Neill LP, Turner BM (mart 2002). "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): 9590–7. doi:10.1074/jbc.M107942200. PMID 11777905.
  46. ^ a b Cai RL, Yan-Neale Y, Cueto MA, Xu H, Cohen D (septembar 2000). "HDAC1, a histone deacetylase, forms a complex with Hus1 and Rad9, two G2/M checkpoint Rad proteins". The Journal of Biological Chemistry. 275 (36): 27909–16. doi:10.1074/jbc.M000168200. PMID 10846170.
  47. ^ a b Fischer DD, Cai R, Bhatia U, Asselbergs FA, Song C, Terry R, Trogani N, Widmer R, Atadja P, Cohen D (februar 2002). "Isolation and characterization of a novel class II histone deacetylase, HDAC10". The Journal of Biological Chemistry. 277 (8): 6656–66. doi:10.1074/jbc.M108055200. PMID 11739383.
  48. ^ Hakimi MA, Dong Y, Lane WS, Speicher DW, Shiekhattar R (februar 2003). "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): 7234–9. doi:10.1074/jbc.M208992200. PMID 12493763.
  49. ^ Fischle W, Dequiedt F, Hendzel MJ, Guenther MG, Lazar MA, Voelter W, Verdin E (januar 2002). "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. doi:10.1016/s1097-2765(01)00429-4. hdl:11858/00-001M-0000-002C-9FF7-D. PMID 11804585.
  50. ^ Fischle W, Dequiedt F, Fillion M, Hendzel MJ, Voelter W, Verdin E (septembar 2001). "Human HDAC7 histone deacetylase activity is associated with HDAC3 in vivo". The Journal of Biological Chemistry. 276 (38): 35826–35. doi:10.1074/jbc.M104935200. PMID 11466315.
  51. ^ a b Ashburner BP, Westerheide SD, Baldwin AS (oktobar 2001). "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): 7065–77. doi:10.1128/MCB.21.20.7065-7077.2001. PMC 99882. PMID 11564889.
  52. ^ a b c d e f g h i Zhang Y, Ng HH, Erdjument-Bromage H, Tempst P, Bird A, Reinberg D (august 1999). "Analysis of the NuRD subunits reveals a histone deacetylase core complex and a connection with DNA methylation". Genes & Development. 13 (15): 1924–35. doi:10.1101/gad.13.15.1924. PMC 316920. PMID 10444591.
  53. ^ a b c Hassig CA, Tong JK, Fleischer TC, Owa T, Grable PG, Ayer DE, Schreiber SL (mart 1998). "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): 3519–24. Bibcode:1998PNAS...95.3519H. doi:10.1073/pnas.95.7.3519. PMC 19868. PMID 9520398.
  54. ^ a b c Zhang Y, Iratni R, Erdjument-Bromage H, Tempst P, Reinberg D (maj 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.
  55. ^ Melhuish TA, Gallo CM, Wotton D (august 2001). "TGIF2 interacts with histone deacetylase 1 and represses transcription". The Journal of Biological Chemistry. 276 (34): 32109–14. doi:10.1074/jbc.M103377200. PMID 11427533.
  56. ^ Wysocka J, Myers MP, Laherty CD, Eisenman RN, Herr W (april 2003). "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. doi:10.1101/gad.252103. PMC 196026. PMID 12670868.
  57. ^ Vietor I, Vadivelu SK, Wick N, Hoffman R, Cotten M, Seiser C, Fialka I, Wunderlich W, Haase A, Korinkova G, Brosch G, Huber LA (septembar 2002). "TIS7 interacts with the mammalian SIN3 histone deacetylase complex in epithelial cells". The EMBO Journal. 21 (17): 4621–31. doi:10.1093/emboj/cdf461. PMC 125408. PMID 12198164.
  58. ^ a b Koipally J, Renold A, Kim J, Georgopoulos K (juni 1999). "Repression by Ikaros and Aiolos is mediated through histone deacetylase complexes". The EMBO Journal. 18 (11): 3090–100. doi:10.1093/emboj/18.11.3090. PMC 1171390. PMID 10357820.
  59. ^ Koipally J, Georgopoulos K (august 2002). "A molecular dissection of the repression circuitry of Ikaros". The Journal of Biological Chemistry. 277 (31): 27697–705. doi:10.1074/jbc.M201694200. PMID 12015313.
  60. ^ Vieyra D, Loewith R, Scott M, Bonnefin P, Boisvert FM, Cheema P, Pastyryeva S, Meijer M, Johnston RN, Bazett-Jones DP, McMahon S, Cole MD, Young D, Riabowol K (august 2002). "Human ING1 proteins differentially regulate histone acetylation". The Journal of Biological Chemistry. 277 (33): 29832–9. doi:10.1074/jbc.M200197200. PMID 12015309.
  61. ^ Sakai H, Urano T, Ookata K, Kim MH, Hirai Y, Saito M, Nojima Y, Ishikawa F (decembar 2002). "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): 48714–23. doi:10.1074/jbc.M208461200. PMID 12354758.
  62. ^ Saito M, Ishikawa F (septembar 2002). "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): 35434–9. doi:10.1074/jbc.M203455200. PMID 12124384.
  63. ^ Ding Z, Gillespie LL, Paterno GD (januar 2003). "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): 250–8. doi:10.1128/mcb.23.1.250-258.2003. PMC 140656. PMID 12482978.
  64. ^ Xia ZB, Anderson M, Diaz MO, Zeleznik-Le NJ (juli 2003). "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): 8342–7. Bibcode:2003PNAS..100.8342X. doi:10.1073/pnas.1436338100. PMC 166231. PMID 12829790.
  65. ^ Mazumdar A, Wang RA, Mishra SK, Adam L, Bagheri-Yarmand R, Mandal M, Vadlamudi RK, Kumar R (januar 2001). "Transcriptional repression of oestrogen receptor by metastasis-associated protein 1 corepressor". Nature Cell Biology. 3 (1): 30–7. doi:10.1038/35050532. PMID 11146623. S2CID 23477845.
  66. ^ a b c d You A, Tong JK, Grozinger CM, Schreiber SL (februar 2001). "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): 1454–8. Bibcode:2001PNAS...98.1454Y. doi:10.1073/pnas.98.4.1454. PMC 29278. PMID 11171972.
  67. ^ a b c Yasui D, Miyano M, Cai S, Varga-Weisz P, Kohwi-Shigematsu T (oktobar 2002). "SATB1 targets chromatin remodelling to regulate genes over long distances". Nature. 419 (6907): 641–5. Bibcode:2002Natur.419..641Y. doi:10.1038/nature01084. PMID 12374985. S2CID 25822700.
  68. ^ Ito A, Kawaguchi Y, Lai CH, Kovacs JJ, Higashimoto Y, Appella E, Yao TP (novembar 2002). "MDM2-HDAC1-mediated deacetylation of p53 is required for its degradation". The EMBO Journal. 21 (22): 6236–45. doi:10.1093/emboj/cdf616. PMC 137207. PMID 12426395.
  69. ^ a b c Ng HH, Zhang Y, Hendrich B, Johnson CA, Turner BM, Erdjument-Bromage H, Tempst P, Reinberg D, Bird A (septembar 1999). "MBD2 is a transcriptional repressor belonging to the MeCP1 histone deacetylase complex". Nature Genetics. 23 (1): 58–61. doi:10.1038/12659. hdl:1842/684. PMID 10471499. S2CID 6147725.
  70. ^ Brackertz M, Boeke J, Zhang R, Renkawitz R (oktobar 2002). "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): 40958–66. doi:10.1074/jbc.M207467200. PMID 12183469.
  71. ^ Wotton D, Lo RS, Lee S, Massagué J (april 1999). "A Smad transcriptional corepressor". Cell. 97 (1): 29–39. doi:10.1016/s0092-8674(00)80712-6. PMID 10199400. S2CID 6907878.
  72. ^ a b Polesskaya A, Rudnicki MA (decembar 2002). "A MyoD-dependent differentiation checkpoint: ensuring genome integrity". Developmental Cell. 3 (6): 757–8. doi:10.1016/s1534-5807(02)00372-6. PMID 12479798.
  73. ^ Mal A, Sturniolo M, Schiltz RL, Ghosh MK, Harter ML (april 2001). "A role for histone deacetylase HDAC1 in modulating the transcriptional activity of MyoD: inhibition of the myogenic program". The EMBO Journal. 20 (7): 1739–53. doi:10.1093/emboj/20.7.1739. PMC 145490. PMID 11285237.
  74. ^ a b Zhong H, May MJ, Jimi E, Ghosh S (mart 2002). "The phosphorylation status of nuclear NF-kappa B determines its association with CBP/p300 or HDAC-1". Molecular Cell. 9 (3): 625–36. doi:10.1016/s1097-2765(02)00477-x. PMID 11931769.
  75. ^ Underhill C, Qutob MS, Yee SP, Torchia J (decembar 2000). "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): 40463–70. doi:10.1074/jbc.M007864200. PMID 11013263.
  76. ^ Zupkovitz, Gordin; Lagger, Sabine; Martin, David; Steiner, Marianne; Hagelkruys, Astrid; Seiser, Christian; Schöfer, Christian; Pusch, Oliver (28. 6. 2018). "Histone deacetylase 1 expression is inversely correlated with age in the short-lived fish Nothobranchius furzeri". Histochemistry and Cell Biology. 150 (3): 255–269. doi:10.1007/s00418-018-1687-4. PMC 6096771. PMID 29951776.
  77. ^ Milutinovic S, Zhuang Q, Szyf M (juni 2002). "Proliferating cell nuclear antigen associates with histone deacetylase activity, integrating DNA replication and chromatin modification". The Journal of Biological Chemistry. 277 (23): 20974–8. doi:10.1074/jbc.M202504200. PMID 11929879.
  78. ^ Iwase S, Januma A, Miyamoto K, Shono N, Honda A, Yanagisawa J, Baba T (septembar 2004). "Characterization of BHC80 in BRAF-HDAC complex, involved in neuron-specific gene repression". Biochemical and Biophysical Research Communications. 322 (2): 601–8. doi:10.1016/j.bbrc.2004.07.163. PMID 15325272.
  79. ^ Joshi B, Ko D, Ordonez-Ercan D, Chellappan SP (decembar 2003). "A putative coiled-coil domain of prohibitin is sufficient to repress E2F1-mediated transcription and induce apoptosis". Biochemical and Biophysical Research Communications. 312 (2): 459–66. doi:10.1016/j.bbrc.2003.10.148. PMID 14637159.
  80. ^ a b Wang S, Fusaro G, Padmanabhan J, Chellappan SP (decembar 2002). "Prohibitin co-localizes with Rb in the nucleus and recruits N-CoR and HDAC1 for transcriptional repression". Oncogene. 21 (55): 8388–96. doi:10.1038/sj.onc.1205944. PMID 12466959.
  81. ^ Khan MM, Nomura T, Kim H, Kaul SC, Wadhwa R, Shinagawa T, Ichikawa-Iwata E, Zhong S, Pandolfi PP, Ishii S (juni 2001). "Role of PML and PML-RARalpha in Mad-mediated transcriptional repression". Molecular Cell. 7 (6): 1233–43. doi:10.1016/s1097-2765(01)00257-x. PMID 11430826.
  82. ^ Wu WS, Vallian S, Seto E, Yang WM, Edmondson D, Roth S, Chang KS (april 2001). "The growth suppressor PML represses transcription by functionally and physically interacting with histone deacetylases". Molecular and Cellular Biology. 21 (7): 2259–68. doi:10.1128/MCB.21.7.2259-2268.2001. PMC 86860. PMID 11259576.
  83. ^ a b Zhang Y, Dufau ML (juni 2003). "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): 401–14. doi:10.1016/s0960-0760(03)00230-9. PMID 12943729. S2CID 28512341.
  84. ^ a b c Zhang Y, Dufau ML (septembar 2002). "Silencing of transcription of the human luteinizing hormone receptor gene by histone deacetylase-mSin3A complex". The Journal of Biological Chemistry. 277 (36): 33431–8. doi:10.1074/jbc.M204417200. PMID 12091390.
  85. ^ Nicolas E, Ait-Si-Ali S, Trouche D (august 2001). "The histone deacetylase HDAC3 targets RbAp48 to the retinoblastoma protein". Nucleic Acids Research. 29 (15): 3131–6. doi:10.1093/nar/29.15.3131. PMC 55834. PMID 11470869.
  86. ^ Hassig CA, Fleischer TC, Billin AN, Schreiber SL, Ayer DE (maj 1997). "Histone deacetylase activity is required for full transcriptional repression by mSin3A". Cell. 89 (3): 341–7. doi:10.1016/s0092-8674(00)80214-7. PMID 9150133. S2CID 14233219.
  87. ^ Kiernan R, Brès V, Ng RW, Coudart MP, El Messaoudi S, Sardet C, Jin DY, Emiliani S, Benkirane M (januar 2003). "Post-activation turn-off of NF-kappa B-dependent transcription is regulated by acetylation of p65". The Journal of Biological Chemistry. 278 (4): 2758–66. doi:10.1074/jbc.M209572200. PMID 12419806.
  88. ^ Anderson LA, Perkins ND (august 2002). "The large subunit of replication factor C interacts with the histone deacetylase, HDAC1". The Journal of Biological Chemistry. 277 (33): 29550–4. doi:10.1074/jbc.M200513200. PMID 12045192.
  89. ^ a b c Ferreira R, Magnaghi-Jaulin L, Robin P, Harel-Bellan A, Trouche D (septembar 1998). "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): 10493–8. Bibcode:1998PNAS...9510493F. doi:10.1073/pnas.95.18.10493. PMC 27922. PMID 9724731.
  90. ^ a b Lai A, Lee JM, Yang WM, DeCaprio JA, Kaelin WG, Seto E, Branton PE (oktobar 1999). "RBP1 recruits both histone deacetylase-dependent and -independent repression activities to retinoblastoma family proteins". Molecular and Cellular Biology. 19 (10): 6632–41. doi:10.1128/mcb.19.10.6632. PMC 84642. PMID 10490602.
  91. ^ Dick FA, Sailhamer E, Dyson NJ (maj 2000). "Mutagenesis of the pRB pocket reveals that cell cycle arrest functions are separable from binding to viral oncoproteins". Molecular and Cellular Biology. 20 (10): 3715–27. doi:10.1128/mcb.20.10.3715-3727.2000. PMC 85672. PMID 10779361.
  92. ^ Fuks F, Burgers WA, Brehm A, Hughes-Davies L, Kouzarides T (januar 2000). "DNA methyltransferase Dnmt1 associates with histone deacetylase activity". Nature Genetics. 24 (1): 88–91. doi:10.1038/71750. PMID 10615135. S2CID 20428600.
  93. ^ Luo RX, Postigo AA, Dean DC (februar 1998). "Rb interacts with histone deacetylase to repress transcription". Cell. 92 (4): 463–73. doi:10.1016/s0092-8674(00)80940-x. PMID 9491888. S2CID 18857544.
  94. ^ Bouzahzah B, Fu M, Iavarone A, Factor VM, Thorgeirsson SS, Pestell RG (august 2000). "Transforming growth factor-beta1 recruits histone deacetylase 1 to a p130 repressor complex in transgenic mice in vivo". Cancer Research. 60 (16): 4531–7. PMID 10969803.
  95. ^ Huang NE, Lin CH, Lin YS, Yu WC (juni 2003). "Modulation of YY1 activity by SAP30". Biochemical and Biophysical Research Communications. 306 (1): 267–75. doi:10.1016/S0006-291X(03)00966-5. PMID 12788099.
  96. ^ Zhang Y, Sun ZW, Iratni R, Erdjument-Bromage H, Tempst P, Hampsey M, Reinberg D (juni 1998). "SAP30, a novel protein conserved between human and yeast, is a component of a histone deacetylase complex". Molecular Cell. 1 (7): 1021–31. doi:10.1016/s1097-2765(00)80102-1. PMID 9651585.
  97. ^ Swanson KA, Knoepfler PS, Huang K, Kang RS, Cowley SM, Laherty CD, Eisenman RN, Radhakrishnan I (august 2004). "HBP1 and Mad1 repressors bind the Sin3 corepressor PAH2 domain with opposite helical orientations". Nature Structural & Molecular Biology. 11 (8): 738–46. doi:10.1038/nsmb798. PMID 15235594. S2CID 44324333.
  98. ^ Yochum GS, Ayer DE (juli 2001). "Pf1, a novel PHD zinc finger protein that links the TLE corepressor to the mSin3A-histone deacetylase complex". Molecular and Cellular Biology. 21 (13): 4110–8. doi:10.1128/MCB.21.13.4110-4118.2001. PMC 87072. PMID 11390640.
  99. ^ a b Fleischer TC, Yun UJ, Ayer DE (maj 2003). "Identification and characterization of three new components of the mSin3A corepressor complex". Molecular and Cellular Biology. 23 (10): 3456–67. doi:10.1128/mcb.23.10.3456-3467.2003. PMC 164750. PMID 12724404.
  100. ^ Yang L, Mei Q, Zielinska-Kwiatkowska A, Matsui Y, Blackburn ML, Benedetti D, Krumm AA, Taborsky GJ, Chansky HA (februar 2003). "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): 651–7. doi:10.1042/BJ20020854. PMC 1223118. PMID 12398767.
  101. ^ Zhang J, Kalkum M, Chait BT, Roeder RG (mart 2002). "The N-CoR-HDAC3 nuclear receptor corepressor complex inhibits the JNK pathway through the integral subunit GPS2". Molecular Cell. 9 (3): 611–23. doi:10.1016/s1097-2765(02)00468-9. PMID 11931768.
  102. ^ Huang EY, Zhang J, Miska EA, Guenther MG, Kouzarides T, Lazar MA (januar 2000). "Nuclear receptor corepressors partner with class II histone deacetylases in a Sin3-independent repression pathway". Genes & Development. 14 (1): 45–54. PMC 316335. PMID 10640275.
  103. ^ Shi Y, Downes M, Xie W, Kao HY, Ordentlich P, Tsai CC, Hon M, Evans RM (maj 2001). "Sharp, an inducible cofactor that integrates nuclear receptor repression and activation". Genes & Development. 15 (9): 1140–51. doi:10.1101/gad.871201. PMC 312688. PMID 11331609.
  104. ^ Alland L, David G, Shen-Li H, Potes J, Muhle R, Lee HC, Hou H, Chen K, DePinho RA (april 2002). "Identification of mammalian Sds3 as an integral component of the Sin3/histone deacetylase corepressor complex". Molecular and Cellular Biology. 22 (8): 2743–50. doi:10.1128/mcb.22.8.2743-2750.2002. PMC 133736. PMID 11909966.
  105. ^ Vaute O, Nicolas E, Vandel L, Trouche D (januar 2002). "Functional and physical interaction between the histone methyl transferase Suv39H1 and histone deacetylases". Nucleic Acids Research. 30 (2): 475–81. doi:10.1093/nar/30.2.475. PMC 99834. PMID 11788710.
  106. ^ Di Padova M, Bruno T, De Nicola F, Iezzi S, D'Angelo C, Gallo R, Nicosia D, Corbi N, Biroccio A, Floridi A, Passananti C, Fanciulli M (septembar 2003). "Che-1 arrests human colon carcinoma cell proliferation by displacing HDAC1 from the p21WAF1/CIP1 promoter". The Journal of Biological Chemistry. 278 (38): 36496–504. doi:10.1074/jbc.M306694200. PMID 12847090.
  107. ^ Singh J, Murata K, Itahana Y, Desprez PY (mart 2002). "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): 1812–22. doi:10.1038/sj.onc.1205252. PMID 11896613.
  108. ^ Sun JM, Chen HY, Moniwa M, Litchfield DW, Seto E, Davie JR (septembar 2002). "The transcriptional repressor Sp3 is associated with CK2-phosphorylated histone deacetylase 2". The Journal of Biological Chemistry. 277 (39): 35783–6. doi:10.1074/jbc.C200378200. PMID 12176973.
  109. ^ a b Tsai SC, Valkov N, Yang WM, Gump J, Sullivan D, Seto E (novembar 2000). "Histone deacetylase interacts directly with DNA topoisomerase II". Nature Genetics. 26 (3): 349–53. doi:10.1038/81671. PMID 11062478. S2CID 19301396.
  110. ^ a b Johnson CA, Padget K, Austin CA, Turner BM (februar 2001). "Deacetylase activity associates with topoisomerase II and is necessary for etoposide-induced apoptosis". The Journal of Biological Chemistry. 276 (7): 4539–42. doi:10.1074/jbc.C000824200. PMID 11136718.
  111. ^ Chauchereau A, Mathieu M, de Saintignon J, Ferreira R, Pritchard LL, Mishal Z, Dejean A, Harel-Bellan A (novembar 2004). "HDAC4 mediates transcriptional repression by the acute promyelocytic leukaemia-associated protein PLZF". Oncogene. 23 (54): 8777–84. doi:10.1038/sj.onc.1208128. PMID 15467736.
  112. ^ Wong CW, Privalsky ML (oktobar 1998). "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): 27695–702. doi:10.1074/jbc.273.42.27695. PMID 9765306.

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