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PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
16
pubmed:dateCreated
2011-7-29
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.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Aug
pubmed:issn
1098-5530
pubmed:author
pubmed:issnType
Electronic
pubmed:volume
193
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
4113-22
pubmed:meshHeading
pubmed:year
2011
pubmed:articleTitle
Alterations in the ? flap and ?' dock domains of the RNA polymerase abolish NusA-mediated feedback regulation of the metY-nusA-infB operon.
pubmed:affiliation
Department of Molecular Biology, Umeå University, SE-901 87 Umeå, Sweden.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't