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An Msh3 ATPase domain mutation has no effect on MMR function.

ABSTRACT: OBJECTIVE:To demonstrate that the Msh3 ATPase domain is required for DNA mismatch repair and tumor suppression in a murine model. RESULTS:The DNA mismatch repair proteins are members of the ABC family of ATPases. ATP binding and hydrolysis regulates their mismatch repair function. In the current study, a mouse model was generated harboring a glycine to aspartic acid residue change in the Walker A motif of the ATPase domain of Msh3. Impaired ATP mediated release of the Msh2-Msh3 GD/GD complex from it's DNA substrate in vitro confirmed the presence of an ATPase defect. However, the mismatch repair function of the protein was not significantly affected. Therefore, mutation of a critical residue within the ATPase domain of Msh3 did not preclude mismatch repair at the genomic sequences tested. Indicating that Msh3 mediated mismatch function is retained the absence of a functional ATPase domain.

SUBMITTER: Edwards Y

PROVIDER: S-EPMC5702223 | biostudies-literature | 2017 Nov

REPOSITORIES: biostudies-literature

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An Msh3 ATPase domain mutation has no effect on MMR function.

Edwards Yasmin Y

BMC research notes 20171125 1

<h4>Objective</h4>To demonstrate that the Msh3 ATPase domain is required for DNA mismatch repair and tumor suppression in a murine model.<h4>Results</h4>The DNA mismatch repair proteins are members of the ABC family of ATPases. ATP binding and hydrolysis regulates their mismatch repair function. In the current study, a mouse model was generated harboring a glycine to aspartic acid residue change in the Walker A motif of the ATPase domain of Msh3. Impaired ATP mediated release of the Msh2-Msh3 <s ...[more]

PMID: 29178930

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