|
rdf:type |
|
|
lifeskim:mentions |
|
|
pubmed:issue |
3
|
|
pubmed:dateCreated |
1999-2-11
|
|
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.
|
|
pubmed:grant |
|
|
pubmed:language |
eng
|
|
pubmed:journal |
|
|
pubmed:citationSubset |
IM
|
|
pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Adenosine Triphosphatases,
http://linkedlifedata.com/resource/pubmed/chemical/Adenosine Triphosphate,
http://linkedlifedata.com/resource/pubmed/chemical/Adenylyl Imidodiphosphate,
http://linkedlifedata.com/resource/pubmed/chemical/Bacterial Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/DNA, Bacterial,
http://linkedlifedata.com/resource/pubmed/chemical/DNA Repair Enzymes,
http://linkedlifedata.com/resource/pubmed/chemical/DNA-Binding Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Endodeoxyribonucleases,
http://linkedlifedata.com/resource/pubmed/chemical/Escherichia coli Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/MutL protein, E coli,
http://linkedlifedata.com/resource/pubmed/chemical/methyl-directed mismatch repair...
|
|
pubmed:status |
MEDLINE
|
|
pubmed:month |
Jan
|
|
pubmed:issn |
0021-9258
|
|
pubmed:author |
|
|
pubmed:issnType |
Print
|
|
pubmed:day |
15
|
|
pubmed:volume |
274
|
|
pubmed:owner |
NLM
|
|
pubmed:authorsComplete |
Y
|
|
pubmed:pagination |
1306-12
|
|
pubmed:dateRevised |
2007-11-14
|
|
pubmed:meshHeading |
pubmed-meshheading:9880500-Adenosine Triphosphatases,
pubmed-meshheading:9880500-Adenosine Triphosphate,
pubmed-meshheading:9880500-Adenylyl Imidodiphosphate,
pubmed-meshheading:9880500-Bacterial Proteins,
pubmed-meshheading:9880500-Base Pair Mismatch,
pubmed-meshheading:9880500-Chromatography, Affinity,
pubmed-meshheading:9880500-DNA, Bacterial,
pubmed-meshheading:9880500-DNA Repair,
pubmed-meshheading:9880500-DNA Repair Enzymes,
pubmed-meshheading:9880500-DNA-Binding Proteins,
pubmed-meshheading:9880500-Endodeoxyribonucleases,
pubmed-meshheading:9880500-Escherichia coli,
pubmed-meshheading:9880500-Escherichia coli Proteins,
pubmed-meshheading:9880500-Hydrolysis
|
|
pubmed:year |
1999
|
|
pubmed:articleTitle |
The Escherichia coli MutL protein physically interacts with MutH and stimulates the MutH-associated endonuclease activity.
|
|
pubmed:affiliation |
Department of Biology, University of North Carolina, Chapel Hill, North Carolina 27599, USA.
|
|
pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.
|
