Nucleotide-promoted Release of hMutSα from Heteroduplex DNA Is Consistent with an ATP-dependent Translocation Mechanism
Author:
Publisher
Elsevier BV
Subject
Cell Biology,Molecular Biology,Biochemistry
Reference27 articles.
1. Altering the conserved nucleotide binding motif in the Salmonella typhimurium MutS mismatch repair protein affects both its ATPase and mismatch binding activities.
2. Initiation of methyl-directed mismatch repair.
3. Dominant negative mutator mutations in the mutS gene of Escherichia coli
4. Genetic and biochemical analysis of Msh2p-Msh6p: role of ATP hydrolysis and Msh2p-Msh6p subunit interactions in mismatch base pair recognition
5. hMSH2 and hMSH6 play distinct roles in mismatch binding and contribute differently to the ATPase activity of hMutSalpha
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