Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1
pubmed:dateCreated
2006-3-24
pubmed:abstractText
Escherichia coli SoxS, the direct transcription activator of the SoxRS (superoxide) regulon, is intrinsically unstable with an in vivo half-life of approximately 2 min. Overexpression of SoxS is lethal, but mutations interfering with DNA binding relieve the toxicity. Here, we determined the effects on the half-life of SoxS of alanine substitutions that confer defects in positive control, i.e. transcription activation, or in specific DNA binding. We found that both types of mutations render SoxS more unstable than the wild-type protein, as if 'soxbox' DNA and RNA polymerase serve as stabilizing ligands in vivo that protect SoxS from degradation by Lon, the protease shown previously to be primarily responsible for its turnover. Indeed, we found that the addition of soxbox DNA or RNA polymerase to an in vitro degradation system decreases the rate of SoxS proteolysis by Lon protease. To the best of our knowledge, these are the first examples of target DNA and RNA polymerase serving as ligands that inhibit the turnover of an unstable transcription activator.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Apr
pubmed:issn
0950-382X
pubmed:author
pubmed:issnType
Print
pubmed:volume
60
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
199-208
pubmed:dateRevised
2007-11-14
pubmed:meshHeading
pubmed:year
2006
pubmed:articleTitle
Inhibition of Lon-dependent degradation of the Escherichia coli transcription activator SoxS by interaction with 'soxbox' DNA or RNA polymerase.
pubmed:affiliation
Department of Biological Sciences, University of Maryland Baltimore County, 1000 Hilltop Circle, Baltimore, MD 21250, USA.
pubmed:publicationType
Journal Article, Research Support, N.I.H., Extramural