| pubmed-article:3104911 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:3104911 | lifeskim:mentions | umls-concept:C0034865 | lld:lifeskim |
| pubmed-article:3104911 | lifeskim:mentions | umls-concept:C1551714 | lld:lifeskim |
| pubmed-article:3104911 | lifeskim:mentions | umls-concept:C0524637 | lld:lifeskim |
| pubmed-article:3104911 | lifeskim:mentions | umls-concept:C0026882 | lld:lifeskim |
| pubmed-article:3104911 | lifeskim:mentions | umls-concept:C1710236 | lld:lifeskim |
| pubmed-article:3104911 | lifeskim:mentions | umls-concept:C0392760 | lld:lifeskim |
| pubmed-article:3104911 | lifeskim:mentions | umls-concept:C0527356 | lld:lifeskim |
| pubmed-article:3104911 | pubmed:issue | 8 | lld:pubmed |
| pubmed-article:3104911 | pubmed:dateCreated | 1987-5-15 | lld:pubmed |
| pubmed-article:3104911 | pubmed:abstractText | The site-specific recombinase encoded by the yeast plasmid 2-microns circle (FLP) forms a transient covalent linkage with its substrate DNA via a tyrosine residue, which appears to be located near its COOH terminus. The homology of the COOH terminus of FLP with that of the Int family of recombinases suggests that tyrosine-343 of FLP could be involved in forming the DNA-protein bridge. We have mutated tyrosine-343 to a phenylalanine or serine. We demonstrate that the binding of each of the two mutant proteins to its substrate is indistinguishable from that of wild-type FLP. However, both mutant proteins are incapable of catalyzing strand cleavage and recombination. | lld:pubmed |
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| pubmed-article:3104911 | pubmed:language | eng | lld:pubmed |
| pubmed-article:3104911 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:3104911 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:3104911 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:3104911 | pubmed:month | Apr | lld:pubmed |
| pubmed-article:3104911 | pubmed:issn | 0027-8424 | lld:pubmed |
| pubmed-article:3104911 | pubmed:author | pubmed-author:YoungL JLJ | lld:pubmed |
| pubmed-article:3104911 | pubmed:author | pubmed-author:JayaramMM | lld:pubmed |
| pubmed-article:3104911 | pubmed:author | pubmed-author:PrasadP VPV | lld:pubmed |
| pubmed-article:3104911 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:3104911 | pubmed:volume | 84 | lld:pubmed |
| pubmed-article:3104911 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:3104911 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:3104911 | pubmed:pagination | 2189-93 | lld:pubmed |
| pubmed-article:3104911 | pubmed:dateRevised | 2009-11-18 | lld:pubmed |
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| pubmed-article:3104911 | pubmed:year | 1987 | lld:pubmed |
| pubmed-article:3104911 | pubmed:articleTitle | Mutations in the 2-microns circle site-specific recombinase that abolish recombination without affecting substrate recognition. | lld:pubmed |
| pubmed-article:3104911 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:3104911 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
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