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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
26
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pubmed:dateCreated |
2003-7-1
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pubmed:abstractText |
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.
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Adenosine Triphosphatases,
http://linkedlifedata.com/resource/pubmed/chemical/Bacterial Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/DNA-Directed RNA Polymerases,
http://linkedlifedata.com/resource/pubmed/chemical/Host Factor 1 Protein,
http://linkedlifedata.com/resource/pubmed/chemical/RNA, Bacterial,
http://linkedlifedata.com/resource/pubmed/chemical/RNA, Messenger,
http://linkedlifedata.com/resource/pubmed/chemical/Recombinant Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Ribonucleoproteins, Small Nuclear,
http://linkedlifedata.com/resource/pubmed/chemical/Ribosomal Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Sigma Factor,
http://linkedlifedata.com/resource/pubmed/chemical/ribosomal protein S1
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pubmed:status |
MEDLINE
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pubmed:month |
Jul
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pubmed:issn |
0006-2960
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
8
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pubmed:volume |
42
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
8022-34
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pubmed:dateRevised |
2006-11-15
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pubmed:meshHeading |
pubmed-meshheading:12834354-Adenosine Triphosphatases,
pubmed-meshheading:12834354-Amino Acid Sequence,
pubmed-meshheading:12834354-Bacterial Proteins,
pubmed-meshheading:12834354-Blotting, Western,
pubmed-meshheading:12834354-DNA-Directed RNA Polymerases,
pubmed-meshheading:12834354-Escherichia coli,
pubmed-meshheading:12834354-Host Factor 1 Protein,
pubmed-meshheading:12834354-Molecular Sequence Data,
pubmed-meshheading:12834354-Plasmids,
pubmed-meshheading:12834354-Protein Binding,
pubmed-meshheading:12834354-Protein Biosynthesis,
pubmed-meshheading:12834354-RNA, Bacterial,
pubmed-meshheading:12834354-RNA, Messenger,
pubmed-meshheading:12834354-Recombinant Proteins,
pubmed-meshheading:12834354-Ribonucleoproteins, Small Nuclear,
pubmed-meshheading:12834354-Ribosomal Proteins,
pubmed-meshheading:12834354-Ribosomes,
pubmed-meshheading:12834354-Sequence Homology, Amino Acid,
pubmed-meshheading:12834354-Sigma Factor,
pubmed-meshheading:12834354-Transcription, Genetic
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pubmed:year |
2003
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pubmed:articleTitle |
Interaction of Escherichia coli RNA polymerase with the ribosomal protein S1 and the Sm-like ATPase Hfq.
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pubmed:affiliation |
Laboratory of Molecular Biology, National Cancer Institute, National Institutes of Health, Bethesda, Maryland 20892, USA. soukhodm@dc37a.nci.nih.gov
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pubmed:publicationType |
Journal Article
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