Affinity of mismatch-binding protein MutS for heteroduplexes containing different mismatches.

Journal article

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.

Authors: Brown, J; Brown, T; Fox, K

• Publication status: Published
• Journal: Biochemical journal
• Volume: 354
• Issue: Pt 3
• Pages: 627-633
• Publication date: 2001-03-01
• DOI: 10.1042/0264-6021:3540627
• EISSN: 1470-8728
• ISSN: 0264-6021
• Language: English
• Keywords: Adenosine Triphosphatases; Nucleic Acid Heteroduplexes; DNA; Base Pair Mismatch; Escherichia coli Proteins; Thymine; Bacterial Proteins; DNA-Binding Proteins; Oligonucleotides; MutS DNA Mismatch-Binding Protein; Guanine