
Mismatch-containing oligonucleotide duplexes bound by the E. coli mutS-encoded protein.
The binding of the mutS gene product, a protein involved in at least two E. coli mismatch correction pathways, to a series of synthetic DNA duplexes containing mismatches or mismatch analogues of the purine/pyrimidine type was studied in order to establish whether a correlation exists between the recognition of these mispairs and the efficiency of their correction in vivo. Experiments using nitrocellulose filter binding or band-shift assays revealed that duplexes containing a G/T mismatch or its analogues I/T and DI/T were bound by the protein with affinities correlating to the efficiency of their repair in vivo. In contrast, the A/C mismatch, contained within the same sequence, was bound only poorly, despite being efficiently corrected in vivo. The analogues of the A/C mispair, uncorrected in vivo, were not detectably bound under the conditions of these assays.
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Related Subject Headings
- Pyrophosphatases
- Phosphoric Monoester Hydrolases
- Oligonucleotides
- Nucleic Acid Heteroduplexes
- Nucleic Acid Conformation
- Genes, Bacterial
- Escherichia coli Proteins
- Escherichia coli
- Developmental Biology
- DNA-Binding Proteins
Citation

Published In
DOI
ISSN
Publication Date
Volume
Issue
Start / End Page
Location
Related Subject Headings
- Pyrophosphatases
- Phosphoric Monoester Hydrolases
- Oligonucleotides
- Nucleic Acid Heteroduplexes
- Nucleic Acid Conformation
- Genes, Bacterial
- Escherichia coli Proteins
- Escherichia coli
- Developmental Biology
- DNA-Binding Proteins