Linked Life Data

14636572

Source:http://linkedlifedata.com/resource/pubmed/id/14636572

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
5
pubmed:dateCreated
2003-11-25
pubmed:abstractText
Bacterial RNA polymerase (RNAP) responds to formation of RNA secondary structures (hairpins) in newly synthesized RNA. Depending on the spacing of the hairpin from the RNA 3' end and the intervening RNA sequence, the hairpin can prolong pausing or cause transcriptional termination. At the his pause site, the pause hairpin contacts a flexible domain on RNAP called the flap, which forms a critical part of a hairpin-interaction site on the enzyme. We report that pause hairpin-flap interaction stabilizes an inhibited configuration of RNAP's active site without changing RNAP's translocation register. The distal part of the flap (the flap tip) is required for the hairpin to affect the active site, but not for hairpin formation. In contrast, the flap tip is not required for intrinsic termination, but can modulate it at suboptimal termination signals.
pubmed:grant
pubmed:commentsCorrections
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Nov
pubmed:issn
1097-2765
pubmed:author
pubmed:issnType
Print
pubmed:volume
12
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
1125-36
pubmed:dateRevised
2007-11-14
pubmed:meshHeading
pubmed:year
2003
pubmed:articleTitle
The flap domain is required for pause RNA hairpin inhibition of catalysis by RNA polymerase and can modulate intrinsic termination.
pubmed:affiliation
Department of Bacteriology, University of Wisconsin, Madison, WI 53706, USA.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S.