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dc.contributor.authorWu, Te-hui
dc.contributor.authorMarinus, Martin G.
dc.date2022-08-11T08:10:04.000
dc.date.accessioned2022-08-23T16:54:04Z
dc.date.available2022-08-23T16:54:04Z
dc.date.issued1999-02-20
dc.date.submitted2008-08-04
dc.identifier.citation<p>J Biol Chem. 1999 Feb 26;274(9):5948-52.</p>
dc.identifier.issn0021-9258 (Print)
dc.identifier.doi10.1074/jbc.274.9.5948
dc.identifier.pmid10026220
dc.identifier.urihttp://hdl.handle.net/20.500.14038/42417
dc.description.abstractThe MutS protein is part of the dam-directed MutHLS mismatch repair pathway in Escherichia coli. We have constructed deletion derivatives in the mutS gene, which retain the P-loop coding region for ATP binding. The mutant proteins were assayed for ATP hydrolysis, heteroduplex DNA binding, heterodimer MutS formation, and the ability to interact with MutL. Dimerization was assayed by expressing His6-tagged wild-type and non-tagged deletion mutant proteins in the same cell and isolating the His6-tagged protein followed by MutS immunoblotting after SDS-polyacrylamide gel electrophoresis. MutS-MutL interaction was measured using the same technique except that the MutL protein carried the His6 tag. Our results indicate that DNA binding ability resides in the N-terminal end of MutS, and dimerization and MutL interactions are located in the C-terminal end. Given the extensive amino acid homology in the MutS family our results with E. coli should be applicable to MutS homologues in other prokaryotes and eukaryotes.
dc.language.isoen_US
dc.relation<p><a href="http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?db=pubmed&cmd=Retrieve&list_uids=10026220&dopt=Abstract">Link to Article in PubMed</a></p>
dc.relation.urlhttps://doi.org/10.1074/jbc.274.9.5948
dc.subject*Adenosine Triphosphatases
dc.subjectAmino Acid Sequence
dc.subjectBacterial Proteins
dc.subjectBase Sequence
dc.subjectDNA Repair
dc.subject*DNA-Binding Proteins
dc.subjectEscherichia coli
dc.subject*Escherichia coli Proteins
dc.subjectMolecular Sequence Data
dc.subjectMutS DNA Mismatch-Binding Protein
dc.subject*Mutation
dc.subjectNucleic Acid Heteroduplexes
dc.subjectProtein Binding
dc.subject*Sequence Deletion
dc.subjectLife Sciences
dc.subjectMedicine and Health Sciences
dc.titleDeletion mutation analysis of the mutS gene in Escherichia coli
dc.typeJournal Article
dc.source.journaltitleThe Journal of biological chemistry
dc.source.volume274
dc.source.issue9
dc.identifier.legacycoverpagehttps://escholarship.umassmed.edu/oapubs/769
dc.identifier.contextkey564684
html.description.abstract<p>The MutS protein is part of the dam-directed MutHLS mismatch repair pathway in Escherichia coli. We have constructed deletion derivatives in the mutS gene, which retain the P-loop coding region for ATP binding. The mutant proteins were assayed for ATP hydrolysis, heteroduplex DNA binding, heterodimer MutS formation, and the ability to interact with MutL. Dimerization was assayed by expressing His6-tagged wild-type and non-tagged deletion mutant proteins in the same cell and isolating the His6-tagged protein followed by MutS immunoblotting after SDS-polyacrylamide gel electrophoresis. MutS-MutL interaction was measured using the same technique except that the MutL protein carried the His6 tag. Our results indicate that DNA binding ability resides in the N-terminal end of MutS, and dimerization and MutL interactions are located in the C-terminal end. Given the extensive amino acid homology in the MutS family our results with E. coli should be applicable to MutS homologues in other prokaryotes and eukaryotes.</p>
dc.identifier.submissionpathoapubs/769
dc.contributor.departmentDepartment of Pharmacology and Molecular Toxicology
dc.source.pages5948-52


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