Interaction of Escherichia coli RNA polymerase with the ribosomal protein S1 and the Sm-like ATPase Hfq

被引:107
作者
Sukhodolets, MV [1 ]
Garges, S [1 ]
机构
[1] NCI, Math Biol Lab, NIH, Bethesda, MD 20892 USA
关键词
D O I
10.1021/bi020638i
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
We report evidence that ribosomal protein S1 and nucleic acid-binding protein Hfq copurify in molar ratios with RNA polymerase (RNAP). Purified SI associates independently with RNAP, and Hfq binding to polymerase occurs in the presence of SI. Looking for a functional role of the RNAP-S1-Hfq association, we studied the effects of S I and Hfq on transcription and coupled transcription-translation. S I was capable of significant stimulation of the RNAP transcriptional activity from a number of promoters; the stimulatory effect was observed on linear as well as supercoiled DNA templates. In addition, we present biochemical and genetic evidence of ATPase activity associated with the Sm-like hexameric nucleic acid-binding protein Hfq. The limited sequence homology between Hfq and known ATP-utilizing enzymes suggests a new class of ATPases.
引用
收藏
页码:8022 / 8034
页数:13
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