Linked Life Data

20875081

Source:http://linkedlifedata.com/resource/pubmed/id/20875081

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
21
pubmed:dateCreated
2010-11-2
pubmed:abstractText
We report here on the formation of a complex between the two NrpR homologs present in Methanosarcina mazei Gö1 and their binding properties to the nifH and glnK(1) promoters. Reciprocal co-chromatography demonstrated that NrpRI forms stable complexes with NrpRII (at an NrpRI : NrpRII molar ratio of ? 1 : 3), which are not affected by 2-oxoglutarate. Promoter-binding, analyses using DNA-affinity chromatography and electrophoretic gel mobility shift assays, verified that NrpRII is not able to bind to either the nifH promoter or the glnK(1) promoter except when in complex with NrpRI. Specific binding of NrpRI to the nifH and glnK(1) promoters was shown to be highly sensitive to 2-oxoglutarate, regardless of whether only NrpRI, or NrpRI in complex with NrpRII, bound to the promoter. Finally, strong interactions between NrpRII and the general transcription factors TATA-binding proteins (TBP) 1-3 and the general transcription factor TFIIB (TFB) were demonstrated, interactions which are also sensitive to 2-oxoglutarate. On the basis of these findings we propose the following: under nitrogen sufficiency NrpRII binds from solution to either the nifH promoter or the glnK(1) promoter by simultaneously contacting NrpRI and TBP plus TFB, resulting in full repression of transcription; whereas, under nitrogen limitation, increasing 2-oxoglutarate concentrations significantly decrease the binding of NrpRI to the operator as well as the binding of NrpRII to TBP and TFB, ultimately allowing recruitment of RNA polymerase to the promoter.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Nov
pubmed:issn
1742-4658
pubmed:author
pubmed:copyrightInfo
© 2010 The Authors Journal compilation © 2010 FEBS.
pubmed:issnType
Electronic
pubmed:volume
277
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
4398-411
pubmed:meshHeading
pubmed-meshheading:20875081-Archaeal Proteins, pubmed-meshheading:20875081-Binding, Competitive, pubmed-meshheading:20875081-Blotting, Western, pubmed-meshheading:20875081-Electrophoretic Mobility Shift Assay, pubmed-meshheading:20875081-Gene Expression Regulation, Archaeal, pubmed-meshheading:20875081-Ketoglutaric Acids, pubmed-meshheading:20875081-Methanosarcina, pubmed-meshheading:20875081-Models, Genetic, pubmed-meshheading:20875081-Nitrogen, pubmed-meshheading:20875081-Oxidoreductases, pubmed-meshheading:20875081-Plasmids, pubmed-meshheading:20875081-Promoter Regions, Genetic, pubmed-meshheading:20875081-Protein Binding, pubmed-meshheading:20875081-Protein Biosynthesis, pubmed-meshheading:20875081-Reverse Transcriptase Polymerase Chain Reaction, pubmed-meshheading:20875081-TATA-Box Binding Protein, pubmed-meshheading:20875081-Transcription Factor TFIIB, pubmed-meshheading:20875081-Transcription Factors
pubmed:year
2010
pubmed:articleTitle
NrpRII mediates contacts between NrpRI and general transcription factors in the archaeon Methanosarcina mazei Gö1.
pubmed:affiliation
Institut für Allgemeine Mikrobiologie, Christian-Albrechts Universität zu Kiel, Kiel, Germany.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't