Mismatch repair: The praying bends of fidelity

Current Biology

Volumn 10, Issue 21, 2000, Pages

  Jiricny, Josef ^a  

^a UNIVERSITY OF ZURICH   (Switzerland)

Author keywords

[No Author keywords available]

Indexed keywords

ESCHERICHIA COLI; THERMUS AQUATICUS;

EID: 0034597548     PISSN: 09609822     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0960-9822(00)00772-7     Document Type: Review

References (15)

1. Mechanisms and biological effects of mismatch repair
2. The crystal structure of DNA mismatch repair protein MutS binding to a GT mismatch
3. Crystal structures of mismatch repair protein MutS and its complex with a substrate DNA
4. Photocross-linking of the NH2-terminal region of Taq MutS protein to the major groove of a heteroduplex DNA
5. A mutation in the MSH6 subunit of the Saccharomyces cerevisiae MSH2-MSH6 complex disrupts mismatch recognition
6. Mismatch recognition and DNA-dependent stimulation of the ATPase activity of hMutSα are abolished by a F432A mutation in the hMSH6 subunit
7. Structural studies of DNA fragments: The G.T wobble base pair in A, B and Z DNA; the G.A base pair in B-DNA
8. 4-methylthymine, or the cisplatin-d(GpG) adduct
9. Superfamily of UvrA-related NTP-binding proteins. Implications for rational classification of recombination/repair systems
10. Crystal structure of the ATP-binding subunit of an ABC transporter
11. MutS mediates heteroduplex loop formation by a translocation mechanism
12. Saccharomyces carevisiae Msh2p and Msh6p ATPase activities are both required during mismatch repair
13. Nucleotide-promoted release of hMutS-α from heteroduplex DNA is consistent with an ATP-dependent translocation mechanism
14. hMSH2-hMSH6 forms a hydrolysis-independent sliding clamp on mismatched DNA
15. Mutation of the magnesium binding site of hMSH6 disables the hMutS-α sliding clamp from translocating along DNA