SUV39H1
Histone-lysine N-methyltransferase SUV39H1 is an enzyme that in humans is encoded by the SUV39H1 gene.[1]
Function
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:
References
- ↑ 1.0 1.1 Aagaard L, Laible G, Selenko P, Schmid M, Dorn R, Schotta G et al. (June 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. PMC 1171278. PMID 10202156.
- ↑ "Entrez Gene: SUV39H1 suppressor of variegation 3-9 homolog 1 (Drosophila)".
- ↑ 3.0 3.1 Zhang CL, McKinsey TA, Olson EN (October 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. PMC 139799. PMID 12242305.
- ↑ 4.0 4.1 Fujita N, Watanabe S, Ichimura T, Tsuruzoe S, Shinkai Y, Tachibana M et al. (June 2003). "Methyl-CpG binding domain 1 (MBD1) interacts with the Suv39h1-HP1 heterochromatic complex for DNA methylation-based transcriptional repression". J. Biol. Chem. 278 (26): 24132–8. doi:10.1074/jbc.M302283200. PMID 12711603.
- ↑ Rual JF, Venkatesan K, Hao T, Hirozane-Kishikawa T, Dricot A, Li N et al. (October 2005). "Towards a proteome-scale map of the human protein-protein interaction network". Nature 437 (7062): 1173–8. doi:10.1038/nature04209. PMID 16189514.
- ↑ Fuks F, Hurd PJ, Deplus R, Kouzarides T (May 2003). "The DNA methyltransferases associate with HP1 and the SUV39H1 histone methyltransferase". Nucleic Acids Res. 31 (9): 2305–12. doi:10.1093/nar/gkg332. PMC 154218. PMID 12711675.
- ↑ 7.0 7.1 7.2 Vaute O, Nicolas E, Vandel L, Trouche D (January 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. PMC 99834. PMID 11788710.
- ↑ Chakraborty S, Sinha KK, Senyuk V, Nucifora G (August 2003). "SUV39H1 interacts with AML1 and abrogates AML1 transactivity. AML1 is methylated in vivo". Oncogene 22 (34): 5229–37. doi:10.1038/sj.onc.1206600. PMID 12917624.
- ↑ Nielsen SJ, Schneider R, Bauer UM, Bannister AJ, Morrison A, O'Carroll D et al. (August 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, Ferreira R, Ait-Si-Ali S, Trouche D (October 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. PMC 99795. PMID 11533237.
- ↑ Firestein R, Cui X, Huie P, Cleary ML (July 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. PMC 85941. 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, van 't Veer LJ, Bernards R (1995). "E2F-5, a new E2F family member that interacts with p130 in vivo". Mol. Cell. Biol. 15 (6): 3082–9. PMC 230539. 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, Suyama A, Sugano S (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) (5): 817–29. PMID 10671371.
- Melcher M, Schmid M, Aagaard L, Selenko P, Laible G, Jenuwein T (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. PMC 85674. 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. PMC 85941. 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, Strahl BD, Sun ZW, Schmid M 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, Mechtler K, Jenuwein T (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. PMC 1083799. PMID 11252719.
- Nielsen SJ, Schneider R, Bauer UM, Bannister AJ, Morrison A, O'Carroll D 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, Ferreira R, Ait-Si-Ali S, Trouche D (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. PMC 99795. 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. PMC 99834. PMID 11788710.
- Schotta G, Ebert A, Krauss V, Fischer A, Hoffmann J, Rea S 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. PMC 125909. PMID 11867540.
- Sewalt RG, Lachner M, Vargas M, Hamer KM, den Blaauwen JL, Hendrix T 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. PMC 133945. 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. PMC 139799. PMID 12242305.
- 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.