| pubmed-article:9220013 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:9220013 | lifeskim:mentions | umls-concept:C0014834 | lld:lifeskim |
| pubmed-article:9220013 | lifeskim:mentions | umls-concept:C0542341 | lld:lifeskim |
| pubmed-article:9220013 | lifeskim:mentions | umls-concept:C0678594 | lld:lifeskim |
| pubmed-article:9220013 | lifeskim:mentions | umls-concept:C2003855 | lld:lifeskim |
| pubmed-article:9220013 | lifeskim:mentions | umls-concept:C0205225 | lld:lifeskim |
| pubmed-article:9220013 | lifeskim:mentions | umls-concept:C0527356 | lld:lifeskim |
| pubmed-article:9220013 | pubmed:issue | 5 | lld:pubmed |
| pubmed-article:9220013 | pubmed:dateCreated | 1997-9-18 | lld:pubmed |
| pubmed-article:9220013 | pubmed:abstractText | XerC and XerD are related 298-amino-acid site-specific recombinases, each of which is responsible for the exchange of one pair of strands in Xer recombination. Both recombinases encode functions necessary for sequence-specific DNA-binding, co-operative XerC/D interactions, synapsis and catalysis. These functions were related to the primary amino acid sequence by constructing and analysing internal and C-terminal XerD deletions. An XerD derivative containing residues 1-233 was proficient in specific DNA binding, but did not interact co-operatively with XerC. Deletion of a further five C-terminal amino acids abolished binding to DNA. Proteins deleted for residues 32-88 and for residues 145-159 were deficient in DNA binding. Deletion of residues 244-281, a region containing amino acids necessary for catalysis, gave a protein that bound to DNA. An XerD derivative containing residues 1-268 retained co-operative interactions with XerC; nevertheless, it did not support XerC strand exchange and was defective in XerD catalysis. Residues 1-283 retain a functional catalytic active site, though a protein lacking the five C-terminal amino acids was still unable to mediate normal in vivo recombination, indicating that these residues are needed for a function that is not directly related to DNA binding or catalysis. | lld:pubmed |
| pubmed-article:9220013 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:9220013 | pubmed:language | eng | lld:pubmed |
| pubmed-article:9220013 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:9220013 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:9220013 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:9220013 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:9220013 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:9220013 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:9220013 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:9220013 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:9220013 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:9220013 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:9220013 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:9220013 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:9220013 | pubmed:month | Jun | lld:pubmed |
| pubmed-article:9220013 | pubmed:issn | 0950-382X | lld:pubmed |
| pubmed-article:9220013 | pubmed:author | pubmed-author:SherrattD JDJ | lld:pubmed |
| pubmed-article:9220013 | pubmed:author | pubmed-author:SpiersA JAJ | lld:pubmed |
| pubmed-article:9220013 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:9220013 | pubmed:volume | 24 | lld:pubmed |
| pubmed-article:9220013 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:9220013 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:9220013 | pubmed:pagination | 1071-82 | lld:pubmed |
| pubmed-article:9220013 | pubmed:dateRevised | 2009-9-29 | lld:pubmed |
| pubmed-article:9220013 | pubmed:meshHeading | pubmed-meshheading:9220013-... | lld:pubmed |
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| pubmed-article:9220013 | pubmed:meshHeading | pubmed-meshheading:9220013-... | lld:pubmed |
| pubmed-article:9220013 | pubmed:meshHeading | pubmed-meshheading:9220013-... | lld:pubmed |
| pubmed-article:9220013 | pubmed:meshHeading | pubmed-meshheading:9220013-... | lld:pubmed |
| pubmed-article:9220013 | pubmed:meshHeading | pubmed-meshheading:9220013-... | lld:pubmed |
| pubmed-article:9220013 | pubmed:meshHeading | pubmed-meshheading:9220013-... | lld:pubmed |
| pubmed-article:9220013 | pubmed:meshHeading | pubmed-meshheading:9220013-... | lld:pubmed |
| pubmed-article:9220013 | pubmed:meshHeading | pubmed-meshheading:9220013-... | lld:pubmed |
| pubmed-article:9220013 | pubmed:meshHeading | pubmed-meshheading:9220013-... | lld:pubmed |
| pubmed-article:9220013 | pubmed:year | 1997 | lld:pubmed |
| pubmed-article:9220013 | pubmed:articleTitle | Relating primary structure to function in the Escherichia coli XerD site-specific recombinase. | lld:pubmed |
| pubmed-article:9220013 | pubmed:affiliation | Department of Biochemistry, University of Oxford, UK. | lld:pubmed |
| pubmed-article:9220013 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:9220013 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
| entrez-gene:947362 | entrezgene:pubmed | pubmed-article:9220013 | lld:entrezgene |
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