Squatrito Massimo, Gorrini Chiara, Amati Bruno
Department of Experimental Oncology, European Institute of Oncology (IEO), IFOM-IEO Campus, Milan 20139, Italy.
Trends Cell Biol. 2006 Sep;16(9):433-42. doi: 10.1016/j.tcb.2006.07.007. Epub 2006 Aug 9.
The Tip60 histone acetyltransferase is part of an evolutionarily conserved multisubunit complex, NuA4, which is recruited by many transcription factors to their target promoters, where it is thought to participate in histone acetylation and transcriptional activation. These transcription factors include tumor promoters and also tumor suppressors, such as p53, which links Tip60 to DNA damage responses. Tip60 also has transcription-independent roles in DNA damage responses. First, independently from NuA4, Tip60 binds the kinases ataxia-telangiectasia mutated (ATM) and DNA-dependent protein kinase catalytic subunit (DNA-PKcs) and participates in their activation by DNA double-strand breaks. Second, NuA4 is recruited to the chromatin surrounding the breaks and, through a series of chromatin modifications, contributes to the dynamics of DNA repair. These molecular activities might endow Tip60 with multiple and potentially antagonistic biological functions.
Tip60组蛋白乙酰转移酶是进化上保守的多亚基复合物NuA4的一部分,许多转录因子将其招募至其靶启动子,据认为它在其中参与组蛋白乙酰化和转录激活。这些转录因子包括肿瘤启动子以及肿瘤抑制因子,如p53,它将Tip60与DNA损伤反应联系起来。Tip60在DNA损伤反应中也具有不依赖转录的作用。首先,Tip60独立于NuA4,与共济失调毛细血管扩张症突变激酶(ATM)和DNA依赖性蛋白激酶催化亚基(DNA-PKcs)结合,并通过DNA双链断裂参与其激活。其次,NuA4被招募至断裂周围的染色质,并通过一系列染色质修饰,促进DNA修复的动态过程。这些分子活性可能赋予Tip60多种且可能相互拮抗的生物学功能。