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We have used bandshift analysis to measure the interaction between the Escherichia coli mismatch-binding protein MutS and synthetic DNA fragments containing all possible DNA mismatches as well as an unpaired T (DeltaT). The order of affinity is found to be DeltaT>GT>GG>AA approximately TT approximately TC>CA>GA>CC>GC. We find that the affinity for GT mismatches is affected by the flanking sequence and decreases in the order G(n)C(n)>(GC)(n)>A(n)T(n)>(AT)(n). Studies with base analogues show good binding to phiT (where phi represents 1',2'-dideoxyribose), but much weaker binding to Gphi.


Journal article


Biochem J

Publication Date





627 - 633


Adenosine Triphosphatases, Bacterial Proteins, Base Pair Mismatch, DNA, DNA-Binding Proteins, Escherichia coli Proteins, Guanine, MutS DNA Mismatch-Binding Protein, Nucleic Acid Heteroduplexes, Oligonucleotides, Thymine