Statements in which the resource exists.
SubjectPredicateObjectContext
pubmed-article:11810257rdf:typepubmed:Citationlld:pubmed
pubmed-article:11810257lifeskim:mentionsumls-concept:C0014834lld:lifeskim
pubmed-article:11810257lifeskim:mentionsumls-concept:C0033684lld:lifeskim
pubmed-article:11810257lifeskim:mentionsumls-concept:C0030946lld:lifeskim
pubmed-article:11810257lifeskim:mentionsumls-concept:C0220908lld:lifeskim
pubmed-article:11810257lifeskim:mentionsumls-concept:C1519316lld:lifeskim
pubmed-article:11810257lifeskim:mentionsumls-concept:C2754013lld:lifeskim
pubmed-article:11810257lifeskim:mentionsumls-concept:C1707391lld:lifeskim
pubmed-article:11810257pubmed:issue5lld:pubmed
pubmed-article:11810257pubmed:dateCreated2002-1-25lld:pubmed
pubmed-article:11810257pubmed:abstractTextTrans-translation is a process that adds a hydrophobic peptide tag to the C-terminus of polypeptides, which causes them to become unstable. We designed a genetic screen to identify factors involved in the degradation of trans-translated products, using the green fluorescent protein (GFP) fused to the trans-translation tag as a reporter. Two screens were devised to identify insertional mutants that stabilize such substrates. Only disruption of the clpX or clpP gene resulted in stabilization of the tagged substrates. The sspB gene product was recently shown to be a specificity-enhancing factor for the ClpXP degradation machine. In the wild-type background, targeted inactivation of the sspB gene failed to stabilize the tagged substrate. These results indicate that the ATP-dependent ClpXP protease is probably the only main component involved in the degradation of cytoplasmic trans-translated proteins in Escherichia coli that can be completely inactivated.lld:pubmed
pubmed-article:11810257pubmed:languageenglld:pubmed
pubmed-article:11810257pubmed:journalhttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:11810257pubmed:citationSubsetIMlld:pubmed
pubmed-article:11810257pubmed:chemicalhttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:11810257pubmed:chemicalhttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:11810257pubmed:chemicalhttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:11810257pubmed:chemicalhttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:11810257pubmed:chemicalhttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:11810257pubmed:chemicalhttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:11810257pubmed:chemicalhttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:11810257pubmed:chemicalhttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:11810257pubmed:chemicalhttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:11810257pubmed:statusMEDLINElld:pubmed
pubmed-article:11810257pubmed:monthJanlld:pubmed
pubmed-article:11810257pubmed:issn1617-4615lld:pubmed
pubmed-article:11810257pubmed:authorpubmed-author:BinevKKlld:pubmed
pubmed-article:11810257pubmed:authorpubmed-author:BodóLLlld:pubmed
pubmed-article:11810257pubmed:authorpubmed-author:BoulocPPlld:pubmed
pubmed-article:11810257pubmed:issnTypePrintlld:pubmed
pubmed-article:11810257pubmed:volume266lld:pubmed
pubmed-article:11810257pubmed:ownerNLMlld:pubmed
pubmed-article:11810257pubmed:authorsCompleteYlld:pubmed
pubmed-article:11810257pubmed:pagination827-31lld:pubmed
pubmed-article:11810257pubmed:dateRevised2006-11-15lld:pubmed
pubmed-article:11810257pubmed:meshHeadingpubmed-meshheading:11810257...lld:pubmed
pubmed-article:11810257pubmed:meshHeadingpubmed-meshheading:11810257...lld:pubmed
pubmed-article:11810257pubmed:meshHeadingpubmed-meshheading:11810257...lld:pubmed
pubmed-article:11810257pubmed:meshHeadingpubmed-meshheading:11810257...lld:pubmed
pubmed-article:11810257pubmed:meshHeadingpubmed-meshheading:11810257...lld:pubmed
pubmed-article:11810257pubmed:meshHeadingpubmed-meshheading:11810257...lld:pubmed
pubmed-article:11810257pubmed:meshHeadingpubmed-meshheading:11810257...lld:pubmed
pubmed-article:11810257pubmed:meshHeadingpubmed-meshheading:11810257...lld:pubmed
pubmed-article:11810257pubmed:meshHeadingpubmed-meshheading:11810257...lld:pubmed
pubmed-article:11810257pubmed:meshHeadingpubmed-meshheading:11810257...lld:pubmed
pubmed-article:11810257pubmed:meshHeadingpubmed-meshheading:11810257...lld:pubmed
pubmed-article:11810257pubmed:meshHeadingpubmed-meshheading:11810257...lld:pubmed
pubmed-article:11810257pubmed:meshHeadingpubmed-meshheading:11810257...lld:pubmed
pubmed-article:11810257pubmed:meshHeadingpubmed-meshheading:11810257...lld:pubmed
pubmed-article:11810257pubmed:meshHeadingpubmed-meshheading:11810257...lld:pubmed
pubmed-article:11810257pubmed:meshHeadingpubmed-meshheading:11810257...lld:pubmed
pubmed-article:11810257pubmed:meshHeadingpubmed-meshheading:11810257...lld:pubmed
pubmed-article:11810257pubmed:year2002lld:pubmed
pubmed-article:11810257pubmed:articleTitleScreening for stabilization of proteins with a trans-translation signature in Escherichia coli selects for inactivation of the ClpXP protease.lld:pubmed
pubmed-article:11810257pubmed:affiliationLaboratoire des Réseaux de Régulations, C.N.R.S./U.M.R. 8621, Institut de Génétique et Microbiologie, Centre Scientifique d'Orsay, Université Paris-Sud, Bâtiment 400, 91405 Orsay Cedex, France.lld:pubmed
pubmed-article:11810257pubmed:publicationTypeJournal Articlelld:pubmed
pubmed-article:11810257pubmed:publicationTypeResearch Support, Non-U.S. Gov'tlld:pubmed
entrez-gene:945082entrezgene:pubmedpubmed-article:11810257lld:entrezgene
entrez-gene:945083entrezgene:pubmedpubmed-article:11810257lld:entrezgene
http://linkedlifedata.com/r...pubmed:referesTopubmed-article:11810257lld:pubmed
http://linkedlifedata.com/r...pubmed:referesTopubmed-article:11810257lld:pubmed