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The Rad51/RadA N-terminal domain activates nucleoprotein filament ATPase activity.
| Content Provider | Semantic Scholar |
|---|---|
| Author | Galkin, Vitold E. Wu, Yan Zhang, Xiao-Ping Qian, Xinguo He, Yujiong Yu, Xiong Heyer, Wolf-Dietrich Luo, Yu Egelman, Edward H. |
| Copyright Year | 2006 |
| Abstract | Proteins in the RecA/RadA/Rad51 family form helical filaments on DNA that function in homologous recombination. While these proteins all have the same highly conserved ATP binding core, the RadA/Rad51 proteins have an N-terminal domain that shows no homology with the C-terminal domain found in RecA. Both the Rad51 N-terminal and RecA C-terminal domains have been shown to bind DNA, but no role for these domains has been established. We show that RadA filaments can be trapped in either an inactive or active conformation with respect to the ATPase and that activation involves a large rotation of the subunit aided by the N-terminal domain. The G103E mutation within the yeast Rad51 N-terminal domain inactivates the filament by failing to make proper contacts between the N-terminal domain and the core. These results show that the N-terminal domains play a regulatory role in filament activation and highlight the modular architecture of the recombination proteins. |
| Starting Page | 602 |
| Ending Page | 602 |
| Page Count | 1 |
| File Format | PDF HTM / HTML |
| Alternate Webpage(s) | http://people.virginia.edu/~ehe2n/RadA_G103E.pdf |
| PubMed reference number | 16765891v1 |
| Volume Number | 14 |
| Issue Number | 6 |
| Journal | Structure |
| Language | English |
| Access Restriction | Open |
| Subject Keyword | Adenosine Triphosphate Cytoskeletal Filaments DNA Repair Protein RAD51 Homolog 1 Homologous Gene Homologous Recombination Inactive - Biochemical Activity Level Mutation Nucleoproteins |
| Content Type | Text |
| Resource Type | Article |
