2003
DOI: 10.1016/j.jmb.2003.10.010
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Formation of a DNA Mismatch Repair Complex Mediated by ATP

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Cited by 55 publications
(103 citation statements)
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“…This faster dissociation rate is still comparable to the rate of formation of S1 ATP -S2 ADP in the ATPase pathway at 0.2-0.3 s −1 ( Figure 5C and Figure 6A). Consistent with our results, the rate constants for mismatched DNA dissociation from E. coli MutS in the presence of ATP range from 0.01 to 0.02 s −1 and are slower than or comparable to the 0.06 s −1 rate constant measured for ATPase activity (21). Thus, we speculate that after ATP binds to the MutS•+T DNA complex, the protein can release the mismatch, but ATP hydrolysis at the S2 subunit allows it to rebind the mismatch (Figure 7).…”
Section: What Is Their Function?supporting
confidence: 90%
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“…This faster dissociation rate is still comparable to the rate of formation of S1 ATP -S2 ADP in the ATPase pathway at 0.2-0.3 s −1 ( Figure 5C and Figure 6A). Consistent with our results, the rate constants for mismatched DNA dissociation from E. coli MutS in the presence of ATP range from 0.01 to 0.02 s −1 and are slower than or comparable to the 0.06 s −1 rate constant measured for ATPase activity (21). Thus, we speculate that after ATP binds to the MutS•+T DNA complex, the protein can release the mismatch, but ATP hydrolysis at the S2 subunit allows it to rebind the mismatch (Figure 7).…”
Section: What Is Their Function?supporting
confidence: 90%
“…+T DNA dissociates from MutS bound to two ATP with a 10-fold faster rate constant (0.077 s −1 ) than from MutS free of nucleotide (0.007 s −1 ) ( Figure 6D; note that because there were no blocks at the ends of linear +T DNA, the measurement reflects MutS dissociation from the mismatch, MutS slipping off the DNA ends, or both, ref 21). This faster dissociation rate is still comparable to the rate of formation of S1 ATP -S2 ADP in the ATPase pathway at 0.2-0.3 s −1 ( Figure 5C and Figure 6A).…”
Section: What Is Their Function?mentioning
confidence: 99%
“…when the mismatch signal and the dGATC hemimethylated site resided on two different DNA duplexes or were separated by a physical barrier such as a four-way DNA junction Schofield et al, 2001 b). In addition, E. coli MutS and MutL were observed to form a stable complex at a mismatch in the presence of ATP (Selmane et al, 2003). In these studies, the activation of MutH was measurable, but modest, and nonspecific DNA binding was a potentially confounding issue.…”
Section: A Ternary Complexmentioning
confidence: 97%
“…Both MutS and MutL bind nonspecifically to DNA, and MutS has an appreciable affinity for DNA ends (Acharya et al, 2003;Plotz et al, 2006Plotz et al, , 2002. While an intact ATPase site in MutLα is not required for its interaction with MutS(α) (Acharya et al, 2003;Selmane et al, 2003), the requirement for ATP binding or hydrolysis by MutS(α) in forming a ternary complex with MutL(α) has been extensively studied, but with no definitive results yet (see Iyer et al, 2006). In addition, DNasel footprinting studies reveal that whereas MutS protects approximately one turn of the DNA helix to either side of the mismatch consistent with the crystal structures, the MutS-MutL interaction in the presence of ATP yields a very large DNasel footprint indicative of multiple proteins bound to the DNA (Grilley et al, 1989;Selmane et al, 2003).…”
Section: A Ternary Complexmentioning
confidence: 99%
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