Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
3
pubmed:dateCreated
2003-11-18
pubmed:abstractText
RNase E is known to affect the turnover of ompA mRNA in a growth rate-dependent manner. Here, we show that this enzyme also plays a role in the temperature-dependent stability of the transcript, thereby maintaining comparable levels of OmpA at 28 and 37 degrees C. An increase in the efficiency of RNase E cleavages at 37 degrees C within the 5(') UTR of the transcript in vitro was found to correlate with a decreased half-life and steady-state level at elevated temperature in vivo. However, measurements of de novo OmpA synthesis and in vitro toeprinting experiments suggest that translation of ompA mRNA is more efficient at 37 degrees C when compared to 28 degrees C. Thus, the enhanced translation apparently counteracts the decreased half-life at elevated temperature. Moreover, we propose that the temperature-dependent inverse correlation between ompA mRNA stability and translation can result from structural changes induced in the 5(') UTR of the transcript.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Nov
pubmed:issn
0006-291X
pubmed:author
pubmed:issnType
Print
pubmed:day
21
pubmed:volume
311
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
604-9
pubmed:dateRevised
2008-10-3
pubmed:meshHeading
pubmed:year
2003
pubmed:articleTitle
Temperature-dependent stability and translation of Escherichia coli ompA mRNA.
pubmed:affiliation
Department of Microbiology and Genetics, University of Vienna, Dr Bohrgasse 9/4, A-1030 Vienna, Austria.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't