| First Author | Carrodeguas JA | Year | 2001 |
| Journal | Mol Cell | Volume | 7 |
| Issue | 1 | Pages | 43-54 |
| PubMed ID | 11172710 | Mgi Jnum | J:67323 |
| Mgi Id | MGI:1930386 | Doi | 10.1016/s1097-2765(01)00153-8 |
| Citation | Carrodeguas JA, et al. (2001) Crystal structure and deletion analysis show that the accessory subunit of mammalian DNA polymerase gamma, Pol gamma B, functions as a homodimer. Mol Cell 7(1):43-54 |
| abstractText | Polymerase gamma, which replicates and repairs mitochondrial DNA, requires the Pol gamma B subunit for processivity. We determined the crystal structure of mouse Pol gamma B, a core component of the mitochondrial replication machinery. Pol gamma B shows high similarity to glycyl-tRNA synthetase and dimerizes through an unusual intermolecular four-helix bundle. A human Pol gamma B mutant lacking the four-helix bundle failed to dimerize in solution or to stimulate the catalytic subunit Pol gamma A, but retained the ability to bind with Pol gamma A to a primer-template construct, indicating that the functional holoenzyme contains two Pol gamma B molecules. Other mutants retained stimulatory activity but lost the ability to bind folded ssDNA. These results suggest that the Pol gamma B dimer contains distinct sites for Pol gamma A binding, dimerization, and DNA binding. |
