Crystal structure of NusG N-terminal (NGN) domain from Methanocaldococcus jannaschii and its interaction with rpoE"

被引：11

作者：

Zhou, Huihao ^{[1
,2
]}

Liu, Qi ^{[1
,2
]}

Gao, Yongxiang ^{[1
,2
]}

Teng, Maikun ^{[1
,2
]}

Niu, Liwen ^{[1
,2
]}

机构：

[1] Chinese Acad Sci, Key Lab Struct Biol, Hefei 230027, Anhui, Peoples R China

[2] Univ Sci & Technol China, Microscale & Sch Life Sci, Hefei Natl Lab Phys Sci, Hefei 230027, Anhui, Peoples R China

来源：

PROTEINS-STRUCTURE FUNCTION AND BIOINFORMATICS | 2009年 / 76卷 / 04期

关键词：

RNA polymerase; transcription factor; archaea; homodimer; docking; RNA-POLYMERASE-II; TRANSCRIPTION ELONGATION-FACTOR; IN-VITRO; PROTEIN; DSIF; COMPLEX; REFINEMENT; SPT4;

D O I：

10.1002/prot.22465

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

Transcription in archaea employs a eukaryotic-type transcription apparatus but uses bacterial-type transcription factors. NusG is one of the few archaeal transcription factors whose orthologs are essential in both bacteria and eukaryotes. Archaeal NusG is composed of only an NusG N-terminal (NGN) domain and a KOW domain, which is similar to bacterial NusG but not to the eukaryotic ortholog, Spt5. However, archaeal NusG was confirmed recently to form a complex with rpoE '' that was similar to the Spt5-Spt4 complex. Thus, archaeal NusG presents hybrid features of Spt5 and bacterial NusG. Here we report the crystal structure of NGN from the archaea Methanocaldococcus jannaschii (MjNGN). MjNGN folds to an alpha-beta-alpha sandwich without the appendant domain of bacterial NGNs, and forms a unique homodimer in crystal and solution. MjNGN alone was found to be sufficient for rpoE '' binding an an MjNGN-rpoE '' model has been constructed by rigid docking.

引用

页码：787 / 793

页数：7

共 29 条

[21] RNA polymerase II elongation factors Spt4p and Spt5p play roles in transcription elongation by RNA polymerase I and rRNA processing [J].