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dc.contributor.authorDrotschmann, Karin
dc.contributor.authorAronshtam, Alexander
dc.contributor.authorFritz, Hans-Joachim
dc.contributor.authorMarinus, Martin G.
dc.date2022-08-11T08:08:00.000
dc.date.accessioned2022-08-23T15:39:11Z
dc.date.available2022-08-23T15:39:11Z
dc.date.issued1998-03-21
dc.date.submitted2009-01-12
dc.identifier.citation<p>Nucleic Acids Res. 1998 Feb 15;26(4):948-53. <a href="http://nar.oxfordjournals.org/cgi/reprint/26/4/948">Link to article on publisher's website</a></p>
dc.identifier.issn0305-1048 (Print)
dc.identifier.pmid9461452
dc.identifier.urihttp://hdl.handle.net/20.500.14038/26107
dc.description.abstractVsr DNA mismatch endonuclease is the key enzyme of very short patch (VSP) DNA mismatch repair and nicks the T-containing strand at the site of a T-G mismatch in a sequence-dependent manner. MutS is part of the mutHLS repair system and binds to diverse mismatches in DNA. The function of the mutL gene product is currently unclear but mutations in the gene abolish mutHLS -dependent repair. The absence of MutL severely reduces VSP repair but does not abolish it. Purified MutL appears to act catalytically to bind Vsr to its substrate; one-hundredth of an equivalent of MutL is sufficient to bring about a significant effect. MutL enhances binding of MutS to its substrate 6-fold but does so in a stoichiometric manner. Mutational studies indicate that the MutL interaction region lies within the N-terminal 330 amino acids and that the MutL multimerization region is at the C-terminal end. MutL mutant monomeric forms can stimulate MutS binding.
dc.language.isoen_US
dc.relation<p><a href="http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?db=pubmed&cmd=Retrieve&list_uids=9461452&dopt=Abstract">Link to Article in PubMed</a></p>
dc.subject*Adenosine Triphosphatases
dc.subjectBacterial Proteins
dc.subjectBase Sequence
dc.subjectDNA
dc.subjectDNA Repair
dc.subject*DNA-Binding Proteins
dc.subjectEndodeoxyribonucleases
dc.subjectEscherichia coli
dc.subject*Escherichia coli Proteins
dc.subjectMolecular Sequence Data
dc.subjectMutS DNA Mismatch-Binding Protein
dc.subjectMutation
dc.subjectNucleic Acid Heteroduplexes
dc.subjectProtein Binding
dc.subjectProtein Conformation
dc.subjectAmino Acids, Peptides, and Proteins
dc.subjectBacteria
dc.subjectBiochemistry, Biophysics, and Structural Biology
dc.subjectGenetic Phenomena
dc.subjectPharmacology, Toxicology and Environmental Health
dc.titleThe Escherichia coli MutL protein stimulates binding of Vsr and MutS to heteroduplex DNA
dc.typeJournal Article
dc.source.journaltitleNucleic acids research
dc.source.volume26
dc.source.issue4
dc.identifier.legacyfulltexthttps://escholarship.umassmed.edu/cgi/viewcontent.cgi?article=1045&amp;context=bmp_pp&amp;unstamped=1
dc.identifier.legacycoverpagehttps://escholarship.umassmed.edu/bmp_pp/46
dc.identifier.contextkey692462
refterms.dateFOA2022-08-23T15:39:11Z
html.description.abstract<p>Vsr DNA mismatch endonuclease is the key enzyme of very short patch (VSP) DNA mismatch repair and nicks the T-containing strand at the site of a T-G mismatch in a sequence-dependent manner. MutS is part of the mutHLS repair system and binds to diverse mismatches in DNA. The function of the mutL gene product is currently unclear but mutations in the gene abolish mutHLS -dependent repair. The absence of MutL severely reduces VSP repair but does not abolish it. Purified MutL appears to act catalytically to bind Vsr to its substrate; one-hundredth of an equivalent of MutL is sufficient to bring about a significant effect. MutL enhances binding of MutS to its substrate 6-fold but does so in a stoichiometric manner. Mutational studies indicate that the MutL interaction region lies within the N-terminal 330 amino acids and that the MutL multimerization region is at the C-terminal end. MutL mutant monomeric forms can stimulate MutS binding.</p>
dc.identifier.submissionpathbmp_pp/46
dc.contributor.departmentDepartment of Biochemistry and Molecular Pharmacology
dc.source.pages948-53


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