| pubmed-article:9880500 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:9880500 | lifeskim:mentions | umls-concept:C0014834 | lld:lifeskim |
| pubmed-article:9880500 | lifeskim:mentions | umls-concept:C0033684 | lld:lifeskim |
| pubmed-article:9880500 | lifeskim:mentions | umls-concept:C1148807 | lld:lifeskim |
| pubmed-article:9880500 | pubmed:issue | 3 | lld:pubmed |
| pubmed-article:9880500 | pubmed:dateCreated | 1999-2-11 | lld:pubmed |
| pubmed-article:9880500 | pubmed:abstractText | All possible pairwise combinations of UvrD, MutL, MutS, and MutH were tested using the yeast two-hybrid system to identify potential interactions involving mismatch repair proteins. A two-hybrid screen previously identified a physical interaction between MutL and UvrD. Although several other known interactions were not observed, a novel interaction between MutL and MutH was detected. A series of truncations from the NH2 and COOH termini of MutL demonstrated that the COOH-terminal 218 amino acids were sufficient for the two-hybrid interaction with MutH. Removal of a small number of residues from either the NH2 or COOH termini of MutH eliminated the two-hybrid interaction with MutL. Protein affinity chromatography experiments confirmed that MutL, but not MutS, physically associates with MutH. Furthermore, MutL greatly stimulated the d(GATC)-specific endonuclease activity of MutH in the absence of MutS and a mispaired base. Stimulation of the MutH-associated endonuclease activity by MutL was dependent on ATP binding but not ATP hydrolysis. Further stimulation of this reaction by MutS required the presence of a DNA mismatch and a hydrolyzable form of ATP. These results suggest that MutL activates the MutH-associated endonuclease activity through a physical interaction during methyl-directed mismatch repair in Escherichia coli. | lld:pubmed |
| pubmed-article:9880500 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:9880500 | pubmed:language | eng | lld:pubmed |
| pubmed-article:9880500 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:9880500 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:9880500 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:9880500 | pubmed:month | Jan | lld:pubmed |
| pubmed-article:9880500 | pubmed:issn | 0021-9258 | lld:pubmed |
| pubmed-article:9880500 | pubmed:author | pubmed-author:HallM CMC | lld:pubmed |
| pubmed-article:9880500 | pubmed:author | pubmed-author:MatsonS WSW | lld:pubmed |
| pubmed-article:9880500 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:9880500 | pubmed:day | 15 | lld:pubmed |
| pubmed-article:9880500 | pubmed:volume | 274 | lld:pubmed |
| pubmed-article:9880500 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:9880500 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:9880500 | pubmed:pagination | 1306-12 | lld:pubmed |
| pubmed-article:9880500 | pubmed:dateRevised | 2007-11-14 | lld:pubmed |
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| pubmed-article:9880500 | pubmed:year | 1999 | lld:pubmed |
| pubmed-article:9880500 | pubmed:articleTitle | The Escherichia coli MutL protein physically interacts with MutH and stimulates the MutH-associated endonuclease activity. | lld:pubmed |
| pubmed-article:9880500 | pubmed:affiliation | Department of Biology, University of North Carolina, Chapel Hill, North Carolina 27599, USA. | lld:pubmed |
| pubmed-article:9880500 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:9880500 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
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