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组蛋白翻译后修饰与DNA损伤响应蛋白招募的调控 被引量:2

Post-translational modification of histones and its role on the recruitments of DNA damage response proteins
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摘要 组蛋白翻译后修饰是细胞DNA损伤早期应答反应的重要内涵,一方面是松弛、开放染色质结构的必要分子调节事件,以便DNA损伤响应蛋白能接近DNA损伤位点;另一方面直接参与DNA损伤修复蛋白招募过程的调控。综述了在DNA损伤信号激发下,发生的组蛋白主要修饰类型,异组蛋白H2AX、H2A.Z在DNA损伤部位与组蛋白置换,及其对DNA损伤响应蛋白招募的调节作用和机制。 Post-translational modification of histones is a critical mechanistic aspect of the early molecular response of cells to DNA damage, which is obligated for loosening the highly compacted chromatins and the access of DNA damage response (DDR) proteins to DNA damage. On the other hand, some modifications of histone proteins directly mediate the processing and regulation of DNA damage signaling and the recruitment of DDR proteins. Here, we overview and discuss the major types of histone modifications triggered by DNA damage signals,the exchanges of histone variants H2AX and H2A.Z with histone proteins in response to DNA damage, and the roles and related mechanisms of histone modifications in the recruitments of DDR proteins onto the DNA damage sites.
作者 刘玲 周平坤
出处 《生命科学》 CSCD 2014年第11期1187-1193,共7页 Chinese Bulletin of Life Sciences
基金 国家高技术研究发展计划(2012AA063501) 国家自然科学基金项目(31370843)
关键词 组蛋白 翻译后修饰 DNA损伤响应 DNA修复 histone protein post-translational modification DNA damage response DNA repair
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  • 1Messner S, Hottiger MO. Histone ADP-ribosylation in DNA repair, replication and transcription. Trends Cell Biol, 2011, 21(9): 534-42.
  • 2Hottiger MO. ADP-ribosylation of histones by ARTD 1: an additional module of the histone code? FEBS Let-t, 2011, 585(11): 1595-9.
  • 3Nathan 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, 2006, 20(8): 966-76.
  • 4Li T, Guan J, Huang Z, et al. RNF168-mediated H2A neddylation antagonizes ubiquitylation of H2A and regu- lates DNA damage repair. J Cell Sci, 2014, 127(Pt 10): 2238-48.
  • 5Ma T, Chert Y, Zhang F, et al. RNF111-dependent ned- dylation activates DNA damage-induced ubiquitination. Mol Cell, 2013, 49(5): 897-907.
  • 6Kothapalli N, Sarath G, Zempleni J. Biotinylation of K12 in histone H4 decreases in response to DNA double-strand breaks in human JAr choriocarcinoma cells. J Nutr, 2005, 135(10): 2337-42.
  • 7Nelson C J, Santos-Rosa H, Kouzarides T. Proline isomeri- zation ofhistone H3 regulates lysine methylation and gene expression. Cell, 2006, 126(5): 905-16.
  • 8Xie Z, Dai J, Dai L, et al. Lysine succinylation and lysine malonylation in histones. Mol Cell Proteomics, 2012, 11(5): 100-7.
  • 9Rogakou EP, Pilch DR, Orr AH, et al. DNA double-stranded breaks induce histone H2AX phosphorylation on serine 139. J Biol Chem, 1998, 273(10): 5858-68.
  • 10Burma S, Chen BP, Murphy M, et al. ATM phosphorylates histone H2AX in response to DNA double-strand breaks. J Biol Chem, 2001, 276(45): 42462-7.

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