SUV39H1

From Wikipedia, the free encyclopedia

Suppressor of variegation 3-9 homolog 1 (Drosophila)

Identifiers

SUV39H1; MG44; SUV39H

External IDs

OMIM: 300254 MGI: 1099440 HomoloGene: 2388

Gene ontology
Molecular Function:	• chromatin binding • protein binding • zinc ion binding • S-adenosylmethionine-dependent methyltransferase activity • transferase activity • histone lysine N-methyltransferase activity (H3-K9 specific)
Cellular Component:	• chromatin • condensed nuclear chromosome • nucleus • chromatin silencing complex
Biological Process:	• chromatin assembly or disassembly • chromatin modification

RNA expression pattern

More reference expression data

Orthologs

Human

Mouse

Refseq

NM_003173 (mRNA)
NP_003164 (protein)

NM_011514 (mRNA)
NP_035644 (protein)

Location

Chr X: 48.44 - 48.45 Mb

Chr X: 7.22 - 7.23 Mb

Pubmed search

[1]

[2]

Suppressor of variegation 3-9 homolog 1 (Drosophila), also known as SUV39H1, is a human gene.

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.^[1]

[edit] References

^ Entrez Gene: SUV39H1 suppressor of variegation 3-9 homolog 1 (Drosophila).

[edit] 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. 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. 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. PMID 9373149.
Aagaard L, Laible G, Selenko P, et al. (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.
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. 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. 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. 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. 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. 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. 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. PMID 12565857.