TFIIH的泛素连接酶活性与对DNA损伤的转录反应
Ubiquitin ligase activity of TFIIH and the transcriptional response to DNA damage.
作者信息
Takagi Yuichiro, Masuda Claudio A, Chang Wei-Hau, Komori Hirofumi, Wang Dong, Hunter Tony, Joazeiro Claudio A P, Kornberg Roger D
机构信息
Department of Structural Biology, School of Medicine, Stanford University, Stanford, California 94305, USA.
出版信息
Mol Cell. 2005 Apr 15;18(2):237-43. doi: 10.1016/j.molcel.2005.03.007.
Core transcription factor (TF) IIH purified from yeast possesses an E3 ubiquitin (Ub) ligase activity, which resides, at least in part, in a RING finger (RNF) domain of the Ssl1 subunit. Yeast strains mutated in the Ssl1 RNF domain are sensitive to ultraviolet (UV) light and to methyl methanesulfonate (MMS). This increased sensitivity to DNA-damaging agents does not reflect a deficiency in nucleotide excision repair. Rather, it correlates with reduced transcriptional induction of genes involved in DNA repair, suggesting that the E3 Ub ligase activity of TFIIH mediates the transcriptional response to DNA damage.
从酵母中纯化得到的核心转录因子（TF）IIH具有E3泛素（Ub）连接酶活性，该活性至少部分存在于Ssl1亚基的一个环状结构域（RNF）中。在Ssl1 RNF结构域发生突变的酵母菌株对紫外线（UV）和甲基磺酸甲酯（MMS）敏感。对DNA损伤剂敏感性的增加并不反映核苷酸切除修复的缺陷。相反，它与参与DNA修复的基因转录诱导的降低相关，这表明TFIIH的E3 Ub连接酶活性介导了对DNA损伤的转录反应。
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