Biology:SUV39H1
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Short description: Protein-coding gene in the species Homo sapiens
 Generic protein structure example |
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] In mouse embryonic stem cells, Suv39h1 expression is repressed by OCT4 protein through the induction of an antisense long non-coding RNA.[3]
Interactions
SUV39H1 has been shown to interact with:
- CBX1,[1]
- CBX5,[4][5][6]
- DNMT3A,[7]
- HDAC1,[8]
- HDAC3,[8]
- HDAC9,[4]
- Histone deacetylase 2,[8]
- MBD1,[5]
- RUNX1,[9]
- Retinoblastoma protein,[10][11] and
- SBF1.[12]
References
- ↑ 1.0 1.1 "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. June 1999. doi:10.1093/emboj/18.7.1923. PMID 10202156.
- ↑ "Entrez Gene: SUV39H1 suppressor of variegation 3-9 homolog 1 (Drosophila)". https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=6839.
- ↑ Bernard, Laure D; Dubois, Agnès; Heurtier, Victor; Fischer, Véronique; Gonzalez, Inma; Chervova, Almira; Tachtsidi, Alexandra; Gil, Noa et al. (28 June 2022). "OCT4 activates a Suv39h1-repressive antisense lncRNA to couple histone H3 Lysine 9 methylation to pluripotency". Nucleic Acids Research 50 (13): 7367–7379. doi:10.1093/nar/gkac550. PMID 35762231.
- ↑ 4.0 4.1 "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. October 2002. doi:10.1128/mcb.22.20.7302-7312.2002. PMID 12242305.
- ↑ 5.0 5.1 "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. June 2003. doi:10.1074/jbc.M302283200. PMID 12711603.
- ↑ "Towards a proteome-scale map of the human protein-protein interaction network". Nature 437 (7062): 1173–8. October 2005. doi:10.1038/nature04209. PMID 16189514. Bibcode: 2005Natur.437.1173R.
- ↑ "The DNA methyltransferases associate with HP1 and the SUV39H1 histone methyltransferase". Nucleic Acids Res. 31 (9): 2305–12. May 2003. doi:10.1093/nar/gkg332. PMID 12711675.
- ↑ 8.0 8.1 8.2 "Functional and physical interaction between the histone methyl transferase Suv39H1 and histone deacetylases". Nucleic Acids Res. 30 (2): 475–81. January 2002. doi:10.1093/nar/30.2.475. PMID 11788710.
- ↑ "SUV39H1 interacts with AML1 and abrogates AML1 transactivity. AML1 is methylated in vivo". Oncogene 22 (34): 5229–37. August 2003. doi:10.1038/sj.onc.1206600. PMID 12917624.
- ↑ "Rb targets histone H3 methylation and HP1 to promoters". Nature 412 (6846): 561–5. August 2001. doi:10.1038/35087620. PMID 11484059. Bibcode: 2001Natur.412..561N.
- ↑ "Transcriptional repression by the retinoblastoma protein through the recruitment of a histone methyltransferase". Mol. Cell. Biol. 21 (19): 6484–94. October 2001. doi:10.1128/mcb.21.19.6484-6494.2001. PMID 11533237.
- ↑ "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. July 2000. doi:10.1128/mcb.20.13.4900-4909.2000. PMID 10848615.
- ↑ Khanal, Prem; Kim, Garam; Lim, Sung‐Chul; Yun, Hyo‐Jeong; Lee, Kwang Youl; Choi, Hoo‐Kyun; Choi, Hong Seok (2013). "Prolyl isomerase Pin1 negatively regulates the stability of SUV39H1 to promote tumorigenesis in breast cancer". The FASEB Journal 27 (11): 4606–4618. doi:10.1096/fj.13-236851. PMID 23934277. https://doi.org/10.1096/fj.13-236851.
Further reading
- "SU(VAR)3-9 is a conserved key function in heterochromatic gene silencing". Genetica 117 (2–3): 149–58. 2003. doi:10.1023/A:1022923508198. PMID 12723694.
- "E2F-5, a new E2F family member that interacts with p130 in vivo". Mol. Cell. Biol. 15 (6): 3082–9. 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): 171–4. 1994. doi:10.1016/0378-1119(94)90802-8. PMID 8125298.
- "Construction and characterization of a full length-enriched and a 5'-end-enriched cDNA library". Gene 200 (1–2): 149–56. 1997. doi:10.1016/S0378-1119(97)00411-3. PMID 9373149.
- "Mitotic phosphorylation of SUV39H1, a novel component of active centromeres, coincides with transient accumulation at mammalian centromeres". J. Cell Sci. 113 (5): 817–29. 2000. doi:10.1242/jcs.113.5.817. PMID 10671371.
- "Structure-function analysis of SUV39H1 reveals a dominant role in heterochromatin organization, chromosome segregation, and mitotic progression". Mol. Cell. Biol. 20 (10): 3728–41. 2000. doi:10.1128/MCB.20.10.3728-3741.2000. PMID 10779362.
- "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. 2000. doi:10.1128/MCB.20.13.4900-4909.2000. PMID 10848615.
- "Phosphorylated and dephosphorylated structures of pig heart, GTP-specific succinyl-CoA synthetase". J. Mol. Biol. 299 (5): 1325–39. 2000. doi:10.1006/jmbi.2000.3807. PMID 10873456.
- "Regulation of chromatin structure by site-specific histone H3 methyltransferases". Nature 406 (6796): 593–9. 2000. doi:10.1038/35020506. PMID 10949293. Bibcode: 2000Natur.406..593R.
- "Methylation of histone H3 lysine 9 creates a binding site for HP1 proteins". Nature 410 (6824): 116–20. 2001. doi:10.1038/35065132. PMID 11242053. Bibcode: 2001Natur.410..116L.
- "Physical association between the histone acetyl transferase CBP and a histone methyl transferase". EMBO Rep. 2 (1): 21–6. 2001. doi:10.1093/embo-reports/kve002. PMID 11252719.
- "Rb targets histone H3 methylation and HP1 to promoters". Nature 412 (6846): 561–5. 2001. doi:10.1038/35087620. PMID 11484059. Bibcode: 2001Natur.412..561N.
- "Transcriptional repression by the retinoblastoma protein through the recruitment of a histone methyltransferase". Mol. Cell. Biol. 21 (19): 6484–94. 2001. doi:10.1128/MCB.21.19.6484-6494.2001. PMID 11533237.
- "Functional and physical interaction between the histone methyl transferase Suv39H1 and histone deacetylases". Nucleic Acids Res. 30 (2): 475–81. 2002. doi:10.1093/nar/30.2.475. PMID 11788710.
- "Central role of Drosophila SU(VAR)3-9 in histone H3-K9 methylation and heterochromatic gene silencing". EMBO J. 21 (5): 1121–31. 2002. doi:10.1093/emboj/21.5.1121. PMID 11867540.
- "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. 2002. doi:10.1128/MCB.22.15.5539-5553.2002. PMID 12101246.
- "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. 2002. doi:10.1128/MCB.22.20.7302-7312.2002. PMID 12242305.
- "Self-interaction of heterochromatin protein 1 is required for direct binding to histone methyltransferase, SUV39H1". Biochem. Biophys. Res. Commun. 301 (2): 287–92. 2003. doi:10.1016/S0006-291X(02)03021-8. PMID 12565857.
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