| First Author | Edwards Y | Year | 2017 |
| Journal | BMC Res Notes | Volume | 10 |
| Issue | 1 | Pages | 616 |
| PubMed ID | 29178930 | Mgi Jnum | J:252313 |
| Mgi Id | MGI:6093263 | Doi | 10.1186/s13104-017-2939-4 |
| Citation | Edwards Y (2017) An Msh3 ATPase domain mutation has no effect on MMR function. BMC Res Notes 10(1):616 |
| abstractText | 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. |
