Structural and sequence comparisons arising from the solution structure of the transcription elongation factor NusG from Thermus thermophilus

被引:26
|
作者
Reay, P
Yamasaki, K
Terada, T
Kuramitsu, S
Shirouzu, M
Yokoyama, S
机构
[1] AIST, Age Dimens Res Ctr, Tsukuba, Ibaraki 3058566, Japan
[2] RIKEN, Genom Sci Ctr, Yokohama, Kanagawa, Japan
[3] Osaka Univ, Grad Sch Sci, Dept Biol, Osaka, Japan
[4] Univ Tokyo, Grad Sch Sci, Dept Biophys & Biochem, Tokyo, Japan
关键词
N-utilization substance G; NMR; KOW motif; Spt5; transcription termination; antitermination;
D O I
10.1002/prot.20054
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
NusG is an essential bacterial protein modulator of transcriptional elongation and termination events, and interacts directly with RNA polymerase and Rho protein. Found also in Archaea, NusG shows stretches of sequence similarity to the eukaryotic transcription elongation factor Spt5. Herein, the three-dimensional solution structure of the bacterial NusG from Thermus thermophilus, which shows 43% amino acid sequence similarity to the Escherichia coli NusG, is described, and a survey of NusG and Spt5 amino acid sequences is presented. Although there is a clear evolutionary and functional relationship between these proteins, it is evident from the structural, sequence, and biochemical data that their binding specificities to both nucleic acids and other proteins differ. (C) 2004 Wiley-Liss Inc.
引用
收藏
页码:40 / 51
页数:12
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