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Suppressor of variegation 3-9 homolog 1 (Drosophila)
Identifiers
Symbols SUV39H1; MG44; SUV39H
External IDs OMIM300254 MGI1099440 HomoloGene2388 GeneCards: SUV39H1 Gene
RNA expression pattern
PBB GE SUV39H1 218619 s at tn.png
More reference expression data
Orthologs
Species Human Mouse
Entrez 6839 20937
Ensembl ENSG00000101945 ENSMUSG00000039231
UniProt O43463 Q3TEW2
RefSeq (mRNA) NM_003173 NM_011514
RefSeq (protein) NP_003164 NP_035644
Location (UCSC) Chr X:
48.44 - 48.45 Mb
Chr X:
7.22 - 7.23 Mb
PubMed search [1] [2]

Histone-lysine N-methyltransferase SUV39H1 is an enzyme that in humans is encoded by the SUV39H1 gene.[1]

This gene is a member of the suppressor of variegation 3-9 homolog family and encodes a protein with a chromodomain and a C-terminal SET domain. This nuclear protein moves to the centromeres during mitosis and functions as a histone methyltransferase, methylating Lys-9 of histone H3. Overall, it plays a vital role in heterochromatin organization, chromosome segregation, and mitotic progression.[2]

Interactions

SUV39H1 has been shown to interact with HDAC9,[3] HDAC1,[4] Histone deacetylase 2,[4] Retinoblastoma protein,[5][6] CBX5,[7][8][3] HDAC3,[4] DNMT3A,[9] MBD1,[7] RUNX1,[10] SBF1[11] and CBX1.[1]

References

  1. ^ a b Aagaard L, Laible G, Selenko P, Schmid M, Dorn R, Schotta G, Kuhfittig S, Wolf A, Lebersorger A, Singh PB, Reuter G, Jenuwein T (Jun 1999). "Functional mammalian homologues of the Drosophila PEV-modifier Su(var)3-9 encode centromere-associated proteins which complex with the heterochromatin component M31". EMBO J 18 (7): 1923–38. doi:10.1093/emboj/18.7.1923. PMID 10202156.  
  2. ^ "Entrez Gene: SUV39H1 suppressor of variegation 3-9 homolog 1 (Drosophila)". http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=6839.  
  3. ^ a b Zhang, Chun Li; McKinsey Timothy A, Olson Eric N (Oct. 2002). "Association of class II histone deacetylases with heterochromatin protein 1: potential role for histone methylation in control of muscle differentiation". Mol. Cell. Biol. (United States) 22 (20): 7302–12. ISSN 0270-7306. PMID 12242305.  
  4. ^ a b c Vaute, Olivier; Nicolas Estelle, Vandel Laurence, Trouche Didier (Jan. 2002). "Functional and physical interaction between the histone methyl transferase Suv39H1 and histone deacetylases". Nucleic Acids Res. (England) 30 (2): 475–81. PMID 11788710.  
  5. ^ 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, Kouzarides T (Aug. 2001). "Rb targets histone H3 methylation and HP1 to promoters". Nature (England) 412 (6846): 561–5. doi:10.1038/35087620. ISSN 0028-0836. PMID 11484034.  
  6. ^ Vandel, L; Nicolas E, Vaute O, Ferreira R, Ait-Si-Ali S, Trouche D (Oct. 2001). "Transcriptional repression by the retinoblastoma protein through the recruitment of a histone methyltransferase". Mol. Cell. Biol. (United States) 21 (19): 6484–94. ISSN 0270-7306. PMID 11533237.  
  7. ^ a b Fujita, Naoyuki; Watanabe Sugiko, Ichimura Takaya, Tsuruzoe Shu, Shinkai Yoichi, Tachibana Makoto, Chiba Tsutomu, Nakao Mitsuyoshi (Jun. 2003). "Methyl-CpG binding domain 1 (MBD1) interacts with the Suv39h1-HP1 heterochromatic complex for DNA methylation-based transcriptional repression". J. Biol. Chem. (United States) 278 (26): 24132–8. doi:10.1074/jbc.M302283200. ISSN 0021-9258. PMID 12711603.  
  8. ^ Rual, Jean-François; Venkatesan Kavitha, Hao Tong, Hirozane-Kishikawa Tomoko, Dricot Amélie, Li Ning, Berriz Gabriel F, Gibbons Francis D, Dreze Matija, Ayivi-Guedehoussou Nono, Klitgord Niels, Simon Christophe, Boxem Mike, Milstein Stuart, Rosenberg Jennifer, Goldberg Debra S, Zhang Lan V, Wong Sharyl L, Franklin Giovanni, Li Siming, Albala Joanna S, Lim Janghoo, Fraughton Carlene, Llamosas Estelle, Cevik Sebiha, Bex Camille, Lamesch Philippe, Sikorski Robert S, Vandenhaute Jean, Zoghbi Huda Y, Smolyar Alex, Bosak Stephanie, Sequerra Reynaldo, Doucette-Stamm Lynn, Cusick Michael E, Hill David E, Roth Frederick P, Vidal Marc (Oct. 2005). "Towards a proteome-scale map of the human protein-protein interaction network". Nature (England) 437 (7062): 1173–8. doi:10.1038/nature04209. PMID 16189514.  
  9. ^ Fuks, François; Hurd Paul J, Deplus Rachel, Kouzarides Tony (May. 2003). "The DNA methyltransferases associate with HP1 and the SUV39H1 histone methyltransferase". Nucleic Acids Res. (England) 31 (9): 2305–12. PMID 12711675.  
  10. ^ Chakraborty, Soumen; Sinha Kislay Kumar, Senyuk Vitalyi, Nucifora Giuseppina (Aug. 2003). "SUV39H1 interacts with AML1 and abrogates AML1 transactivity. AML1 is methylated in vivo". Oncogene (England) 22 (34): 5229–37. doi:10.1038/sj.onc.1206600. ISSN 0950-9232. PMID 12917624.  
  11. ^ Firestein, R; Cui X, Huie P, Cleary M L (Jul. 2000). "Set domain-dependent regulation of transcriptional silencing and growth control by SUV39H1, a mammalian ortholog of Drosophila Su(var)3-9". Mol. Cell. Biol. (UNITED STATES) 20 (13): 4900–9. ISSN 0270-7306. PMID 10848615.  

Further reading

  • Schotta G, Ebert A, Reuter G (2003). "SU(VAR)3-9 is a conserved key function in heterochromatic gene silencing.". Genetica 117 (2-3): 149–58. doi:10.1023/A:1022923508198. PMID 12723694.  
  • Hijmans EM, Voorhoeve PM, Beijersbergen RL, et al. (1995). "E2F-5, a new E2F family member that interacts with p130 in vivo.". Mol. Cell. Biol. 15 (6): 3082–9. PMID 7760804.  
  • Maruyama K, Sugano S (1994). "Oligo-capping: a simple method to replace the cap structure of eukaryotic mRNAs with oligoribonucleotides.". Gene 138 (1-2): 171–4. doi:10.1016/0378-1119(94)90802-8. PMID 8125298.  
  • Suzuki Y, Yoshitomo-Nakagawa K, Maruyama K, et al. (1997). "Construction and characterization of a full length-enriched and a 5'-end-enriched cDNA library.". Gene 200 (1-2): 149–56. doi:10.1016/S0378-1119(97)00411-3. PMID 9373149.  
  • Aagaard L, Schmid M, Warburton P, Jenuwein T (2000). "Mitotic phosphorylation of SUV39H1, a novel component of active centromeres, coincides with transient accumulation at mammalian centromeres.". J. Cell. Sci. 113 ( Pt 5): 817–29. PMID 10671371.  
  • Melcher M, Schmid M, Aagaard L, et al. (2000). "Structure-function analysis of SUV39H1 reveals a dominant role in heterochromatin organization, chromosome segregation, and mitotic progression.". Mol. Cell. Biol. 20 (10): 3728–41. doi:10.1128/MCB.20.10.3728-3741.2000. PMID 10779362.  
  • Firestein R, Cui X, Huie P, Cleary ML (2000). "Set domain-dependent regulation of transcriptional silencing and growth control by SUV39H1, a mammalian ortholog of Drosophila Su(var)3-9.". Mol. Cell. Biol. 20 (13): 4900–9. doi:10.1128/MCB.20.13.4900-4909.2000. PMID 10848615.  
  • Fraser ME, James MN, Bridger WA, Wolodko WT (2000). "Phosphorylated and dephosphorylated structures of pig heart, GTP-specific succinyl-CoA synthetase.". J. Mol. Biol. 299 (5): 1325–39. doi:10.1006/jmbi.2000.3807. PMID 10873456.  
  • Rea S, Eisenhaber F, O'Carroll D, et al. (2000). "Regulation of chromatin structure by site-specific histone H3 methyltransferases.". Nature 406 (6796): 593–9. doi:10.1038/35020506. PMID 10949293.  
  • Lachner M, O'Carroll D, Rea S, et al. (2001). "Methylation of histone H3 lysine 9 creates a binding site for HP1 proteins.". Nature 410 (6824): 116–20. doi:10.1038/35065132. PMID 11242053.  
  • Vandel L, Trouche D (2001). "Physical association between the histone acetyl transferase CBP and a histone methyl transferase.". EMBO Rep. 2 (1): 21–6. doi:10.1093/embo-reports/kve002. PMID 11252719.  
  • Nielsen SJ, Schneider R, Bauer UM, et al. (2001). "Rb targets histone H3 methylation and HP1 to promoters.". Nature 412 (6846): 561–5. doi:10.1038/35087620. PMID 11484059.  
  • Vandel L, Nicolas E, Vaute O, et al. (2001). "Transcriptional repression by the retinoblastoma protein through the recruitment of a histone methyltransferase.". Mol. Cell. Biol. 21 (19): 6484–94. doi:10.1128/MCB.21.19.6484-6494.2001. PMID 11533237.  
  • Vaute O, Nicolas E, Vandel L, Trouche D (2002). "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.  
  • Schotta G, Ebert A, Krauss V, et al. (2002). "Central role of Drosophila SU(VAR)3-9 in histone H3-K9 methylation and heterochromatic gene silencing.". Embo J. 21 (5): 1121–31. doi:10.1093/emboj/21.5.1121. PMID 11867540.  
  • Sewalt RG, Lachner M, Vargas M, et al. (2002). "Selective interactions between vertebrate polycomb homologs and the SUV39H1 histone lysine methyltransferase suggest that histone H3-K9 methylation contributes to chromosomal targeting of Polycomb group proteins.". Mol. Cell. Biol. 22 (15): 5539–53. doi:10.1128/MCB.22.15.5539-5553.2002. PMID 12101246.  
  • Zhang CL, McKinsey TA, Olson EN (2002). "Association of class II histone deacetylases with heterochromatin protein 1: potential role for histone methylation in control of muscle differentiation.". Mol. Cell. Biol. 22 (20): 7302–12. doi:10.1128/MCB.22.20.7302-7312.2002. PMID 12242305.  
  • Strausberg RL, Feingold EA, Grouse LH, et al. (2003). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences.". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–903. doi:10.1073/pnas.242603899. PMID 12477932.  
  • Yamamoto K, Sonoda M (2003). "Self-interaction of heterochromatin protein 1 is required for direct binding to histone methyltransferase, SUV39H1.". Biochem. Biophys. Res. Commun. 301 (2): 287–92. doi:10.1016/S0006-291X(02)03021-8. PMID 12565857.  
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