New functional sites in MutS affect DNA mismatch repair

• Published in: Science China. Life sciences Vol. 53; no. 10; pp. 1170 - 1173
• Main Authors: Zhong, TianYing, Bi, LiJun, Zhang, XianEn
• Format: Journal Article
• Language: English
• Published: Beijing Science China Press 01-10-2010; Springer Nature B.V
• Subjects: Adenosine Triphosphatases - metabolism; Binding Sites - genetics; Biomedical and Life Sciences; Blotting, Far-Western; Chromatography, Gel; DNA Mismatch Repair - genetics; DNA Mismatch Repair - physiology; DNA, Bacterial - genetics; DNA, Bacterial - metabolism; Escherichia coli - genetics; Escherichia coli - metabolism; Escherichia coli Proteins - chemistry; Escherichia coli Proteins - genetics; Escherichia coli Proteins - metabolism; Genes, Bacterial; Life Sciences; Mutagenesis; Mutant Proteins - chemistry; Mutant Proteins - genetics; Mutant Proteins - metabolism; Mutation; MutL Proteins; MutS DNA Mismatch-Binding Protein - chemistry; MutS DNA Mismatch-Binding Protein - genetics; MutS DNA Mismatch-Binding Protein - metabolism; Protein Interaction Domains and Motifs; Protein Multimerization; Short Communications; Surface Plasmon Resonance; functional defective mutants; MutS; random mutation; DNA mismatch repair
• ISSN: 1674-7305; 1869-1889
• DOI: 10.1007/s11427-010-4065-6

The MutS protein plays an important role in the DNA mismatch repair system. Mutations in the
mutS
gene can lead to genome instability and ultimately cell malfunction. Here we have established a method for identifying functional defective mutants of MutS by random mutation and rifampicin screening. Some novel functional sites in MutS were identified. The MutS mutant strains were analyzed using surface plasmon resonance, gel filtration and far-western methods to determine the molecular mechanisms behind the DNA mismatch repair function of MutS.