mutS Antibody

1. Mechanism for verification of mismatched and homoduplex DNAs by nucleotides-bound MutS analyzed by molecular dynamics simulations has been reported. PMID: 27238299
2. The assembly of an EcMutS-EcMutL-EcMutH search complex illustrates how sequential stable sliding clamps can modulate one-dimensional diffusion mechanics along the DNA to direct mismatch repair PMID: 27851738
3. The structure captures MutS in the sliding clamp conformation, where tilting of the MutS subunits across each other pushes DNA into a new channel, and reorientation of the connector domain creates an interface for MutL with both MutS subunits. PMID: 26163658
4. MutS and MutL trap recombination intermediates using mismatches formed in the heteroduplex region and secondary DNA structures in the displaced ssDNA, and recruit the UvrD helicase to resolve these trapped intermediates in a directional manner PMID: 23932715
5. E. coli MutS has a binding activity specific for non-B form G4 DNA, but such binding appears independent of canonical heteroduplex repair activation. PMID: 22747774
6. The results confirm that specifically bound MutS bends DNA at the mismatch. PMID: 22367846
7. The Mismatch repair mechanism that involves more MutL accumulation relative to MutS was observed in this study. PMID: 22241777
8. analysis of the dynamic MutS-MutL complex formed in DNA mismatch repair in Escherichia coli PMID: 21454657
9. mismatch recognition by the MutS proteins is linked to these disparate biological outcomes through regulated interaction of MutL proteins with a wide variety of effector proteins PMID: 20667509
10. 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 PMID: 20953938
11. identify a region in the connector domain (domain II) of MutS that binds MutL and is required for mispair-dependent ternary complex formation and mismatch repair PMID: 20080788
12. The C-terminal end of MutS is necessary for antirecombination and cisplatin sensitization, but less significant for mutation avoidance during DNA mismatch repair. PMID: 15731339
13. MutS glutamate 38 plays a role in both DNA mismatch discrimination and in the authorization of repair. PMID: 16407973
14. a beta sliding clamp binds to multiple sites within MutL and MutS PMID: 16546997
15. Results support the hypothesis that tetramerization of MutS is important but not essential for MutS function in DNA mismatch repair. PMID: 17012287
16. Results show that the interaction of MutY and MutS involves the Fe-S domain of MutY and the ATPase domain of MutS and defend against the mutagenic effect of 8-oxoG lesions in a cooperative manner. PMID: 17114250
17. DNA bending could play a role in MutS biochemical modulations induced by a compound lesion and that cisplatin DNA damage signaling by the mismatch repair system could be modulated in a direct mode. PMID: 17400248
18. Since movement of MutS along the chain does not require ATP hydrolysis and the ATPase activity is enhanced when MutS dissociates from a heteroduplex, this support model in which ATP binding by MutS induces the formation of a sliding clamp. PMID: 17950245
19. The data reveal that the loop plays a direct role in co-ordinating conformational changes involved in long-range communication between Walker box and mismatch recognition domains. PMID: 18673453
20. study describes normal-mode calculations of MutS with and without DNA; distinct conformational states are proposed for DNA scanning, mismatch recognition, repair initiation, and sliding along DNA after mismatch recognition PMID: 19254532
21. analysis of MutS-, and MutL-dependent activation of MutH and their roles in methyl-directed mismatch repair in vitro PMID: 19783657

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KEGG: ecj:JW2703

STRING: 316385.ECDH10B_2901