| Title | The BRCA2-interacting protein DSS1 is vital for DNA repair, recombination, and genome stability in Ustilago maydis. |
| Publication Type | Journal Article |
| Year of Publication | 2003 |
| Authors | Kojic M, Yang H, Kostrub CF, Pavletich NP, Holloman WK |
| Journal | Mol Cell |
| Volume | 12 |
| Issue | 4 |
| Pagination | 1043-9 |
| Date Published | 2003 Oct |
| ISSN | 1097-2765 |
| Keywords | BRCA2 Protein, DNA Repair, DNA-Binding Proteins, Evolution, Molecular, Fungal Proteins, Genomic Instability, Meiosis, Molecular Sequence Data, Mutation, Proteins, Rad51 Recombinase, Recombination, Genetic, Sequence Homology, Amino Acid, Sequence Homology, Nucleic Acid, Ustilago |
| Abstract | DSS1 encodes a small acidic protein shown in recent structural studies to interact with the DNA binding domain of BRCA2. Here we report that an ortholog of DSS1 is present in Ustilago maydis and associates with Brh2, the BRCA2-related protein, thus recapitulating the protein partnership in this genetically amenable fungus. Mutants of U. maydis deleted of DSS1 are extremely radiation sensitive, deficient in recombination, defective in meiosis, and disturbed in genome stability; these phenotypes mirror previous observations of U. maydis mutants deficient in Brh2 or Rad51. These findings conclusively show that Dss1 constitutes a protein with a significant role in the recombinational repair pathway in U. maydis, and imply that it plays a similar key role in the recombination systems of organisms in which recombinational repair is BRCA2 dependent. |
| Alternate Journal | Mol. Cell |
| PubMed ID | 14580353 |
| Grant List | GM42482 / GM / NIGMS NIH HHS / United States |
Submitted by mam2155 on March 24, 2014 - 4:14pm