Journal
BIOCHEMISTRY
Volume 42, Issue 26, Pages 8022-8034Publisher
AMER CHEMICAL SOC
DOI: 10.1021/bi020638i
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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.
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