PMID:12834354

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Citation

Sukhodolets, MV and Garges, S (2003) Interaction of Escherichia coli RNA polymerase with the ribosomal protein S1 and the Sm-like ATPase Hfq. Biochemistry 42:8022-34

Abstract

We report evidence that ribosomal protein S1 and nucleic acid-binding protein Hfq copurify in molar ratios with RNA polymerase (RNAP). Purified S1 associates independently with RNAP, and Hfq binding to polymerase occurs in the presence of S1. Looking for a functional role of the RNAP-S1-Hfq association, we studied the effects of S1 and Hfq on transcription and coupled transcription-translation. S1 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.

Links

PubMed Online version:10.1021/bi020638i

Keywords

Adenosine Triphosphatases/metabolism; Amino Acid Sequence; Bacterial Proteins/genetics; Bacterial Proteins/metabolism; Blotting, Western; DNA-Directed RNA Polymerases/genetics; DNA-Directed RNA Polymerases/metabolism; Escherichia coli/enzymology; Escherichia coli/metabolism; Host Factor 1 Protein/genetics; Host Factor 1 Protein/metabolism; Molecular Sequence Data; Plasmids; Protein Binding; Protein Biosynthesis; RNA, Bacterial/metabolism; RNA, Messenger/genetics; RNA, Messenger/metabolism; Recombinant Proteins/isolation & purification; Recombinant Proteins/metabolism; Ribonucleoproteins, Small Nuclear/genetics; Ribonucleoproteins, Small Nuclear/metabolism; Ribosomal Proteins/genetics; Ribosomal Proteins/metabolism; Ribosomes/metabolism; Sequence Homology, Amino Acid; Sigma Factor/metabolism; Transcription, Genetic

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