組蛋白修飾酶

組蛋白修飾酶（Histone-modifying enzymes）泛指真核生物細胞中修飾包裹DNA的組蛋白之酵素。組蛋白上的許多位點可被酵素修飾^[1]，共同組成組蛋白密碼^[2]。已知的修飾種類包括乙醯化^[3]、甲基化^[4]、磷酸化^[5]、泛素化^[6]、GlcNAc糖基化（英语：GlcNAc）^[7]、二磷酸腺苷核糖基化^[8]、瓜氨酸化^[9]、脯胺酸異構化（英语：Proline isomerization in epigenetics）^[10]與SUMO修飾（英语：SUMO protein）等^[11]，這些修飾可能改變染色體結構或與其他蛋白結合的能力，進而促進或抑制基因的轉錄^[2]。

參見

參考文獻

^ Kouzarides T. Chromatin modifications and their function. Cell. February 2007, 128 (4): 693–705. PMID 17320507. doi:10.1016/j.cell.2007.02.005.
^ ^2.0 ^2.1 Jenuwein T, Allis C. Translating the histone code. Science. 2001, 293 (5532): 1074–80. PMID 11498575. doi:10.1126/science.1063127.
^ Sterner DE, Berger SL. Acetylation of histones and transcription-related factors. Microbiol. Mol. Biol. Rev. June 2000, 64 (2): 435–59. PMC 98999 . PMID 10839822. doi:10.1128/MMBR.64.2.435-459.2000.
^ Zhang Y, Reinberg D. Transcription regulation by histone methylation: interplay between different covalent modifications of the core histone tails. Genes Dev. 2001, 15 (18): 2343–60. PMID 11562345. doi:10.1101/gad.927301.
^ Nowak SJ, Corces VG. Phosphorylation of histone H3: a balancing act between chromosome condensation and transcriptional activation. Trends Genet. April 2004, 20 (4): 214–20. PMID 15041176. doi:10.1016/j.tig.2004.02.007.
^ Shilatifard A. Chromatin modifications by methylation and ubiquitination: implications in the regulation of gene expression. Annu. Rev. Biochem. 2006, 75: 243–69. PMID 16756492. doi:10.1146/annurev.biochem.75.103004.142422.
^ K, Sakabe; Z, Wang; Gw, Hart. Beta-N-acetylglucosamine (O-GlcNAc) Is Part of the Histone Code. Proceedings of the National Academy of Sciences of the United States of America. 2010-11-16, 107 (46): 19915–20. Bibcode:2010PNAS..10719915S. PMC 2993388 . PMID 21045127. doi:10.1073/pnas.1009023107.
^ Hassa PO, Haenni SS, Elser M, Hottiger MO. Nuclear ADP-ribosylation reactions in mammalian cells: where are we today and where are we going?. Microbiol. Mol. Biol. Rev. September 2006, 70 (3): 789–829. PMC 1594587 . PMID 16959969. doi:10.1128/MMBR.00040-05.
^ Cuthbert GL, Daujat S, Snowden AW, et al. Histone deimination antagonizes arginine methylation. Cell. September 2004, 118 (5): 545–53. PMID 15339660. doi:10.1016/j.cell.2004.08.020.
^ Nelson CJ, Santos-Rosa H, Kouzarides T. Proline isomerization of histone H3 regulates lysine methylation and gene expression. Cell. September 2006, 126 (5): 905–16. PMID 16959570. doi:10.1016/j.cell.2006.07.026.
^ Nathan D, Ingvarsdottir K, Sterner DE, et al. Histone sumoylation is a negative regulator in Saccharomyces cerevisiae and shows dynamic interplay with positive-acting histone modifications. Genes Dev. April 2006, 20 (8): 966–76. PMC 1472304 . PMID 16598039. doi:10.1101/gad.1404206.

[1] Kouzarides T. Chromatin modifications and their function. Cell. February 2007, 128 (4): 693–705. PMID 17320507. doi:10.1016/j.cell.2007.02.005.

[Jenuwein-2] 2.0 ^2.1 Jenuwein T, Allis C. Translating the histone code. Science. 2001, 293 (5532): 1074–80. PMID 11498575. doi:10.1126/science.1063127.

[3] Sterner DE, Berger SL. Acetylation of histones and transcription-related factors. Microbiol. Mol. Biol. Rev. June 2000, 64 (2): 435–59. PMC 98999 . PMID 10839822. doi:10.1128/MMBR.64.2.435-459.2000.

[4] Zhang Y, Reinberg D. Transcription regulation by histone methylation: interplay between different covalent modifications of the core histone tails. Genes Dev. 2001, 15 (18): 2343–60. PMID 11562345. doi:10.1101/gad.927301.

[5] Nowak SJ, Corces VG. Phosphorylation of histone H3: a balancing act between chromosome condensation and transcriptional activation. Trends Genet. April 2004, 20 (4): 214–20. PMID 15041176. doi:10.1016/j.tig.2004.02.007.

[6] Shilatifard A. Chromatin modifications by methylation and ubiquitination: implications in the regulation of gene expression. Annu. Rev. Biochem. 2006, 75: 243–69. PMID 16756492. doi:10.1146/annurev.biochem.75.103004.142422.

[7] K, Sakabe; Z, Wang; Gw, Hart. Beta-N-acetylglucosamine (O-GlcNAc) Is Part of the Histone Code. Proceedings of the National Academy of Sciences of the United States of America. 2010-11-16, 107 (46): 19915–20. Bibcode:2010PNAS..10719915S. PMC 2993388 . PMID 21045127. doi:10.1073/pnas.1009023107.

[8] Hassa PO, Haenni SS, Elser M, Hottiger MO. Nuclear ADP-ribosylation reactions in mammalian cells: where are we today and where are we going?. Microbiol. Mol. Biol. Rev. September 2006, 70 (3): 789–829. PMC 1594587 . PMID 16959969. doi:10.1128/MMBR.00040-05.

[9] Cuthbert GL, Daujat S, Snowden AW, et al. Histone deimination antagonizes arginine methylation. Cell. September 2004, 118 (5): 545–53. PMID 15339660. doi:10.1016/j.cell.2004.08.020.

[10] Nelson CJ, Santos-Rosa H, Kouzarides T. Proline isomerization of histone H3 regulates lysine methylation and gene expression. Cell. September 2006, 126 (5): 905–16. PMID 16959570. doi:10.1016/j.cell.2006.07.026.

[11] Nathan D, Ingvarsdottir K, Sterner DE, et al. Histone sumoylation is a negative regulator in Saccharomyces cerevisiae and shows dynamic interplay with positive-acting histone modifications. Genes Dev. April 2006, 20 (8): 966–76. PMC 1472304 . PMID 16598039. doi:10.1101/gad.1404206.

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