Crystallographic analysis of the conserved C-terminal domain of transcription factor Cdc73 from Saccharomyces cerevisiae reveals a GTPase-like fold
Crystallographic analysis of the conserved C-terminal domain of transcription factor Cdc73 from Saccharomyces cerevisiae reveals a GTPase-like fold
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对酿酒酵母转录因子 Cdc73 保守 C 端结构域的晶体学分析揭示了 GTP 酶样折叠。
DOI：
10.1107/s0907444912017325
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发表时间：
2012-08-01
影响因子：
2.2
通讯作者：
Niu, Liwen
中科院分区：
文献类型：
--
作者：
Chen, Hongkai;Shi, Nuo;Niu, Liwen
酵母Paf1复合体（Paf1C）由蛋白Paf1、Cdc73、Ctr9、Leo1和Rtf1组成，伴随RNA聚合酶II从启动子到达mRNA和snorna编码基因的3'端形成位点。酵母Cdc73 （yCdc73）是最早发现的Paf1C亚基之一，参与许多转录相关过程，包括与RNA聚合酶II的结合、组蛋白修饰因子的募集和激活以及与其他转录激活因子的通讯。yCdc73的人类同源物parafibromin已被确定为与乳腺癌、肾癌和胃癌相关的肿瘤抑制因子。然而，直到最近，yCdc73的功能机制还不清楚。本文报道了yCdc73高度保守的c端区2.2 Å分辨率的晶体结构。它揭示了yCdc73似乎有一个类似gtpase的折叠。然而，未观察到GTPase活性。yCdc73的晶体结构将为Cdc73和Paf1C的功能模式提供新的思路。
The yeast Paf1 complex (Paf1C), which is composed of the proteins Paf1, Cdc73, Ctr9, Leo1 and Rtf1, accompanies RNA polymerase II from the promoter to the 3'-end formation site of mRNA- and snoRNA-encoding genes. As one of the first identified subunits of Paf1C, yeast Cdc73 (yCdc73) takes part in many transcription-related processes, including binding to RNA polymerase II, recruitment and activation of histone-modification factors and communication with other transcriptional activators. The human homologue of yCdc73, parafibromin, has been identified as a tumour suppressor linked to breast, renal and gastric cancers. However, the functional mechanism of yCdc73 has until recently been unclear. Here, a 2.2 Å resolution crystal structure of the highly conserved C-terminal region of yCdc73 is reported. It revealed that yCdc73 appears to have a GTPase-like fold. However, no GTPase activity was observed. The crystal structure of yCdc73 will shed new light on the modes of function of Cdc73 and Paf1C.