人类Rtf1 Plus3结构域的结构与DNA结合

Structure and DNA binding of the human Rtf1 Plus3 domain.

作者信息

de Jong Rob N, Truffault Vincent, Diercks Tammo, Ab Eiso, Daniels Mark A, Kaptein Rob, Folkers Gert E

机构信息

Bijvoet Centre for Biomolecular Research, Utrecht University, Faculty of Chemistry, Department NMR Spectroscopy, Padualaan 8, Utrecht, The Netherlands.

出版信息

Structure. 2008 Jan;16(1):149-59. doi: 10.1016/j.str.2007.10.018.

DOI:10.1016/j.str.2007.10.018

PMID:18184592

Abstract

The yeast Paf1 complex consists of Paf1, Rtf1, Cdc73, Ctr9, and Leo1 and regulates histone H2B ubiquitination, histone H3 methylation, RNA polymerase II 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 beta 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.

摘要

酵母Paf1复合物由Paf1、Rtf1、Cdc73、Ctr9和Leo1组成，可调节组蛋白H2B泛素化、组蛋白H3甲基化、RNA聚合酶II羧基末端结构域（CTD）Ser2磷酸化以及RNA 3'末端加工。我们通过解析人Rtf1保守且功能重要的Plus3结构域的核磁共振结构，深入了解了Paf1复合物。一个主要由β链组成的亚结构域与Dicer/Argonaute PAZ结构域以及Tudor结构域在结构上具有相似性。我们进一步证明，高度碱性的Rtf1 Plus3结构域在体外可通过β折叠边缘的残基与单链DNA相互作用，这与PAZ结构域结合小干扰RNA（siRNA）的情况类似，但未检测到其与双链DNA或RNA的结合。我们讨论了Rtf1 Plus3与单链DNA结合在转录延伸过程中的潜在作用。