Linked Life Data

11273713

Source:http://linkedlifedata.com/resource/pubmed/id/11273713

Statements in which the resource exists.
SubjectPredicateObjectContext
pubmed-article:11273713rdf:typepubmed:Citationlld:pubmed
pubmed-article:11273713lifeskim:mentionsumls-concept:C0524637lld:lifeskim
pubmed-article:11273713lifeskim:mentionsumls-concept:C1274040lld:lifeskim
pubmed-article:11273713lifeskim:mentionsumls-concept:C0597304lld:lifeskim
pubmed-article:11273713lifeskim:mentionsumls-concept:C1514562lld:lifeskim
pubmed-article:11273713lifeskim:mentionsumls-concept:C1883221lld:lifeskim
pubmed-article:11273713lifeskim:mentionsumls-concept:C0243102lld:lifeskim
pubmed-article:11273713lifeskim:mentionsumls-concept:C2587213lld:lifeskim
pubmed-article:11273713lifeskim:mentionsumls-concept:C1883204lld:lifeskim
pubmed-article:11273713lifeskim:mentionsumls-concept:C1521840lld:lifeskim
pubmed-article:11273713lifeskim:mentionsumls-concept:C1880389lld:lifeskim
pubmed-article:11273713pubmed:issue3lld:pubmed
pubmed-article:11273713pubmed:dateCreated2001-3-29lld:pubmed
pubmed-article:11273713pubmed:abstractTextWe report a genetic and biochemical analysis of a target recognition domain (TRD) of EcoKI, a type I restriction and modification enzyme. The TRDs of type I R-M systems are within the specificity subunit (HsdS) and HsdS confers sequence specificity to a complex endowed with both restriction and modification activities. Random mutagenesis has revealed that most substitutions within the amino TRD of EcoKI, a region comprising 157 amino acid residues, have no detectable effect on the phenotype of the bacterium, even when the substitutions are non- conservative. The structure of the TRD appears to be robust. All but one of the six substitutions that confer a restriction-deficient, modification-deficient (r(-)m(-)) phenotype were found to be in the interval between residues 80 and 110, a region predicted by sequence comparisons to form part of the protein-DNA interface. Additional site-directed mutations affecting this interval commonly impair both restriction and modification. However, we show that an r(-) phenotype cannot be taken as evidence that the EcoKI complex lacks endonuclease activity; in response to even a slightly impaired modification efficiency, the endonuclease activity of EcoKI is destroyed by a process dependent upon the ClpXP protease. Enzymes from mutants with an r(-)m(-) phenotype commonly retain some sequence-specific activity; methylase activity can be detected on hemimethylated DNA substrates and residual endonuclease activity is implied whenever the viability of the r(-)m(-) bacterium is dependent on ClpXP. Conversely, the viability of ClpX(-) r(-)m(-) bacteria can be used as evidence for little, or no, endonuclease activity. Of 14 mutants with an r(-)m(-) phenotype, only six are viable in the absence of ClpXP. The significance of four of the six residues (G91, G105, F107 and G141) is enhanced by the finding that even conservative substitutions for these residues impair modification, thereby conferring an r(-)m(-) phenotype.lld:pubmed
pubmed-article:11273713pubmed:languageenglld:pubmed
pubmed-article:11273713pubmed:journalhttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:11273713pubmed:citationSubsetIMlld:pubmed
pubmed-article:11273713pubmed:chemicalhttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:11273713pubmed:chemicalhttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:11273713pubmed:chemicalhttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:11273713pubmed:chemicalhttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:11273713pubmed:chemicalhttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:11273713pubmed:chemicalhttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:11273713pubmed:chemicalhttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:11273713pubmed:chemicalhttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:11273713pubmed:chemicalhttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:11273713pubmed:chemicalhttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:11273713pubmed:statusMEDLINElld:pubmed
pubmed-article:11273713pubmed:monthMarlld:pubmed
pubmed-article:11273713pubmed:issn0022-2836lld:pubmed
pubmed-article:11273713pubmed:authorpubmed-author:O'NeillMMlld:pubmed
pubmed-article:11273713pubmed:authorpubmed-author:MurrayN ENElld:pubmed
pubmed-article:11273713pubmed:authorpubmed-author:PowellL MLMlld:pubmed
pubmed-article:11273713pubmed:copyrightInfoCopyright 2001 Academic Press.lld:pubmed
pubmed-article:11273713pubmed:issnTypePrintlld:pubmed
pubmed-article:11273713pubmed:day30lld:pubmed
pubmed-article:11273713pubmed:volume307lld:pubmed
pubmed-article:11273713pubmed:ownerNLMlld:pubmed
pubmed-article:11273713pubmed:authorsCompleteYlld:pubmed
pubmed-article:11273713pubmed:pagination951-63lld:pubmed
pubmed-article:11273713pubmed:dateRevised2009-11-3lld:pubmed
pubmed-article:11273713pubmed:meshHeadingpubmed-meshheading:11273713...lld:pubmed
pubmed-article:11273713pubmed:meshHeadingpubmed-meshheading:11273713...lld:pubmed
pubmed-article:11273713pubmed:meshHeadingpubmed-meshheading:11273713...lld:pubmed
pubmed-article:11273713pubmed:meshHeadingpubmed-meshheading:11273713...lld:pubmed
pubmed-article:11273713pubmed:meshHeadingpubmed-meshheading:11273713...lld:pubmed
pubmed-article:11273713pubmed:meshHeadingpubmed-meshheading:11273713...lld:pubmed
pubmed-article:11273713pubmed:meshHeadingpubmed-meshheading:11273713...lld:pubmed
pubmed-article:11273713pubmed:meshHeadingpubmed-meshheading:11273713...lld:pubmed
pubmed-article:11273713pubmed:meshHeadingpubmed-meshheading:11273713...lld:pubmed
pubmed-article:11273713pubmed:meshHeadingpubmed-meshheading:11273713...lld:pubmed
pubmed-article:11273713pubmed:meshHeadingpubmed-meshheading:11273713...lld:pubmed
pubmed-article:11273713pubmed:meshHeadingpubmed-meshheading:11273713...lld:pubmed
pubmed-article:11273713pubmed:meshHeadingpubmed-meshheading:11273713...lld:pubmed
pubmed-article:11273713pubmed:meshHeadingpubmed-meshheading:11273713...lld:pubmed
pubmed-article:11273713pubmed:meshHeadingpubmed-meshheading:11273713...lld:pubmed
pubmed-article:11273713pubmed:meshHeadingpubmed-meshheading:11273713...lld:pubmed
pubmed-article:11273713pubmed:meshHeadingpubmed-meshheading:11273713...lld:pubmed
pubmed-article:11273713pubmed:meshHeadingpubmed-meshheading:11273713...lld:pubmed
pubmed-article:11273713pubmed:meshHeadingpubmed-meshheading:11273713...lld:pubmed
pubmed-article:11273713pubmed:meshHeadingpubmed-meshheading:11273713...lld:pubmed
pubmed-article:11273713pubmed:meshHeadingpubmed-meshheading:11273713...lld:pubmed
pubmed-article:11273713pubmed:year2001lld:pubmed
pubmed-article:11273713pubmed:articleTitleTarget recognition by EcoKI: the recognition domain is robust and restriction-deficiency commonly results from the proteolytic control of enzyme activity.lld:pubmed
pubmed-article:11273713pubmed:affiliationInstitute of Cell and Molecular Biology, University of Edinburgh, Darwin Building, Mayfield Road, King's Buildings, Edinburgh, EH9 3JR, UK.lld:pubmed
pubmed-article:11273713pubmed:publicationTypeJournal Articlelld:pubmed
entrez-gene:945082entrezgene:pubmedpubmed-article:11273713lld:entrezgene
entrez-gene:945083entrezgene:pubmedpubmed-article:11273713lld:entrezgene
http://linkedlifedata.com/r...pubmed:referesTopubmed-article:11273713lld:pubmed
http://linkedlifedata.com/r...pubmed:referesTopubmed-article:11273713lld:pubmed
http://linkedlifedata.com/r...pubmed:referesTopubmed-article:11273713lld:pubmed
http://linkedlifedata.com/r...pubmed:referesTopubmed-article:11273713lld:pubmed
http://linkedlifedata.com/r...pubmed:referesTopubmed-article:11273713lld:pubmed
http://linkedlifedata.com/r...pubmed:referesTopubmed-article:11273713lld:pubmed
http://linkedlifedata.com/r...pubmed:referesTopubmed-article:11273713lld:pubmed
http://linkedlifedata.com/r...pubmed:referesTopubmed-article:11273713lld:pubmed