Source:http://linkedlifedata.com/resource/pubmed/id/21685293
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
16
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pubmed:dateCreated |
2011-7-29
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pubmed:abstractText |
The RimM protein in Escherichia coli is important for the in vivo maturation of 30S ribosomal subunits and a ?rimM mutant grows poorly due to assembly and translational defects. These deficiencies are suppressed partially by mutations that increase the synthesis of another assembly protein, RbfA, encoded by the metY-nusA-infB operon. Among these suppressors are mutations in nusA that impair the NusA-mediated negative-feedback regulation at internal intrinsic transcriptional terminators of the metY-nusA-infB operon. We describe here the isolation of two new mutations, one in rpoB and one in rpoC (encoding the ? and ?' subunits of the RNA polymerase, respectively), that increase the synthesis of RbfA by preventing NusA from stimulating termination at the internal intrinsic transcriptional terminators of the metY-nusA-infB operon. The rpoB2063 mutation changed the isoleucine in position 905 of the ? flap-tip helix to a serine, while the rpoC2064 mutation duplicated positions 415 to 416 (valine-isoleucine) at the base of the ?' dock domain. These findings support previously published in vitro results, which have suggested that the ? flap-tip helix and ?' dock domain at either side of the RNA exit tunnel mediate the binding to NusA during transcriptional pausing and termination.
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pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/DNA-Directed RNA Polymerases,
http://linkedlifedata.com/resource/pubmed/chemical/Escherichia coli Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Peptide Elongation Factors,
http://linkedlifedata.com/resource/pubmed/chemical/Prokaryotic Initiation Factor-2,
http://linkedlifedata.com/resource/pubmed/chemical/Ribosomal Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/RimM protein, E coli,
http://linkedlifedata.com/resource/pubmed/chemical/Transcription Factors,
http://linkedlifedata.com/resource/pubmed/chemical/nusA protein, E coli
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pubmed:status |
MEDLINE
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pubmed:month |
Aug
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pubmed:issn |
1098-5530
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pubmed:author | |
pubmed:issnType |
Electronic
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pubmed:volume |
193
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
4113-22
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pubmed:meshHeading |
pubmed-meshheading:21685293-DNA-Directed RNA Polymerases,
pubmed-meshheading:21685293-Escherichia coli,
pubmed-meshheading:21685293-Escherichia coli Proteins,
pubmed-meshheading:21685293-Gene Expression Regulation, Bacterial,
pubmed-meshheading:21685293-Mutation,
pubmed-meshheading:21685293-Operon,
pubmed-meshheading:21685293-Peptide Elongation Factors,
pubmed-meshheading:21685293-Prokaryotic Initiation Factor-2,
pubmed-meshheading:21685293-Protein Structure, Tertiary,
pubmed-meshheading:21685293-Ribosomal Proteins,
pubmed-meshheading:21685293-Transcription, Genetic,
pubmed-meshheading:21685293-Transcription Factors
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pubmed:year |
2011
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pubmed:articleTitle |
Alterations in the ? flap and ?' dock domains of the RNA polymerase abolish NusA-mediated feedback regulation of the metY-nusA-infB operon.
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pubmed:affiliation |
Department of Molecular Biology, Umeå University, SE-901 87 Umeå, Sweden.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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