Abstract
The methyl-directed long patch repair pathway in Escherichia coli is involved in increasing the fidelity of replication specific repair of DNA polymerase incorporation errors. This pathway is mediated by three gene products, MutS, MutL, and MutH, which are conserved in higher eukaryotes. Mutations in human homologues of these proteins have been shown to be implicated in hereditary non-polyposis colorectal cancer (HNPCC). A MutS homologue has recently been identified in the extremely thermophilic bacterium, Thermus thermophilus. Here we describe analysis of the binding properties of this protein, which has indicated it can identify all specific base mismatches as well as one, two and three base pair insertion/deletion mutations. We therefore believe this protein may be generally useful for applications involving mismatch detection.
Publication types
-
Research Support, Non-U.S. Gov't
MeSH terms
-
Adenosine Triphosphatases*
-
Bacterial Proteins / genetics*
-
Bacterial Proteins / isolation & purification
-
Bacterial Proteins / metabolism*
-
Base Sequence
-
Cloning, Molecular
-
Colorectal Neoplasms / genetics
-
DNA Repair / genetics*
-
DNA, Bacterial / genetics
-
DNA, Bacterial / metabolism
-
DNA-Binding Proteins*
-
Escherichia coli / genetics
-
Escherichia coli / metabolism
-
Escherichia coli Proteins*
-
Gene Expression
-
Genes, Bacterial
-
Humans
-
MutS DNA Mismatch-Binding Protein
-
Mutation
-
Oligodeoxyribonucleotides / genetics
-
Oligodeoxyribonucleotides / metabolism
-
Polymerase Chain Reaction
-
Protein Binding
-
Thermus thermophilus / genetics*
-
Thermus thermophilus / metabolism*
Substances
-
Bacterial Proteins
-
DNA, Bacterial
-
DNA-Binding Proteins
-
Escherichia coli Proteins
-
Oligodeoxyribonucleotides
-
Adenosine Triphosphatases
-
MutS DNA Mismatch-Binding Protein
-
MutS protein, E coli