Structure and DNA binding of the human Rtf1 Plus3 domain

被引：52

作者：

de Jong, Rob N. ^{[1
]}

Truffault, Vincent

Diercks, Tammo ^{[1
]}

AB, Eiso ^{[1
]}

Daniels, Mark A. ^{[1
]}

Kaptein, Rob ^{[1
]}

Folkers, Gert E. ^{[1
]}

机构：

[1] Univ Utrecht, Bijvoet Ctr Biomol Res, Fac Chem, Dept NMR Spectroscopy, NL-3584 CH Utrecht, Netherlands

来源：

STRUCTURE | 2008年 / 16卷 / 01期

关键词：

D O I：

10.1016/j.str.2007.10.018

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 [生物化学与分子生物学]; 081704 [应用化学];

摘要：

The yeast Paf1 complex consists of Paf1, Rtf1, Cdc73, Ctr9, and Leo1 and regulates histone H2B ubiquitination, histone H3 methylation, RNA polymerase 11 carboxy-terminal domain (CTD) Ser2 phosphorylation, and RNA 3' end processing. We provide structural insight into the Paf1 complex with the NMR structure of the conserved and functionally important Plus3 domain of human Rtf1. A predominantly beta-stranded subdomain displays structural similarity to Dicer/Argonaute PAZ domains and to Tudor domains. We further demonstrate that the highly basic Rtf1 Plus3 domain can interact in vitro with single-stranded DNA via residues on the rim of the 0 sheet, reminiscent of siRNA binding by PAZ domains, but did not detect binding to double-stranded DNA or RNA. We discuss the potential role of Rtf1 Plus3 ssDNA binding during transcription elongation.

引用

页码：149 / 159

页数：11

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