Linked Life Data

8764397

Source:http://linkedlifedata.com/resource/pubmed/id/8764397

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
2
pubmed:dateCreated
1996-9-13
pubmed:abstractText
The Bacillus subtilis transcription factor sigma F is a cell-type specific regulatory protein whose activity is governed by SpoIIAB and SpoIIAA and the nucleotides ATP and ADP. SpoIIAB is an anti-sigma factor that binds to sigma F in a manner that is stimulated by ATP, thereby trapping sigma F in an inactive complex. Alternatively, SpoIIAB binds to SpoIIAA in a manner that is stimulated by ADP to form a SpoIIAB.SpoIIAA complex in which SpoIIAB is sequestered from sigma F. SpoIIAB is also a protein kinase that uses ATP to phosphorylate, and thereby inactivate, SpoIIAA. Thus, ATP inhibits sigma F activity both by promoting formation of the SpoIIAB.sigma F complex and by phosphorylation of SpoIIAA. In extension of previous results, we use affinity chromatography to show that SpoIIAB is capable of forming long-lived complexes with sigma F and SpoIIAA and that the formation of these complexes is dependent on ATP and ADP, respectively. Using a DNA template lacking adenosine residues on the non-transcribed strand, we demonstrate that ATP is required for SpoIIAB-mediated inhibition of sigma F-directed RNA synthesis and that this inhibition is prevented by SpoIIAA in a manner that is stimulated by ADP. We show that ADP acts by protecting SpoIIAA from phosphorylation by SpoIIAB and that a mutant protein bearing an amino acid substitution at the site of phosphorylation in SpoIIAA is capable of preventing the inhibition of sigma F in a manner that does not depend on ADP. A principal finding from the investigation is that SpoIIAA restores activity to sigma F that had previously been inhibited by SpoIIAB. This is demonstrated both by the capacity of SpoIIAA to reverse SpoIIAB-mediated inhibition of sigma F-directed RNA synthesis and by its capacity to interact with and disrupt the SpoIIAB. sigma F complex. The results are consistent with a model in which sigma F is controlled by the cellular concentration of unphosphorylated SpoIIAA.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jul
pubmed:issn
0022-2836
pubmed:author
pubmed:issnType
Print
pubmed:day
12
pubmed:volume
260
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
147-64
pubmed:dateRevised
2007-11-14
pubmed:meshHeading
pubmed-meshheading:8764397-Adenosine Diphosphate, pubmed-meshheading:8764397-Adenosine Triphosphate, pubmed-meshheading:8764397-Bacillus subtilis, pubmed-meshheading:8764397-Bacterial Proteins, pubmed-meshheading:8764397-Base Sequence, pubmed-meshheading:8764397-Chromatography, Affinity, pubmed-meshheading:8764397-Cloning, Molecular, pubmed-meshheading:8764397-Electrophoresis, Polyacrylamide Gel, pubmed-meshheading:8764397-Escherichia coli, pubmed-meshheading:8764397-Models, Genetic, pubmed-meshheading:8764397-Molecular Sequence Data, pubmed-meshheading:8764397-Mutagenesis, Site-Directed, pubmed-meshheading:8764397-Phosphorylation, pubmed-meshheading:8764397-Protein Binding, pubmed-meshheading:8764397-Protein Conformation, pubmed-meshheading:8764397-Sigma Factor, pubmed-meshheading:8764397-Transcription, Genetic, pubmed-meshheading:8764397-Transcription Factors
pubmed:year
1996
pubmed:articleTitle
SpoIIAA governs the release of the cell-type specific transcription factor sigma F from its anti-sigma factor SpoIIAB.
pubmed:affiliation
Department of Molecular and Cellular Biology, Harvard University, Cambridge, MA 02138, USA.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S., Research Support, Non-U.S. Gov't