| First Author | Maga G | Year | 2013 |
| Journal | Proc Natl Acad Sci U S A | Volume | 110 |
| Issue | 47 | Pages | 18850-5 |
| PubMed ID | 24191025 | Mgi Jnum | J:202983 |
| Mgi Id | MGI:5523730 | Doi | 10.1073/pnas.1308760110 |
| Citation | Maga G, et al. (2013) DNA polymerase delta-interacting protein 2 is a processivity factor for DNA polymerase lambda during 8-oxo-7,8-dihydroguanine bypass. Proc Natl Acad Sci U S A 110(47):18850-5 |
| abstractText | The bypass of DNA lesions by the replication fork requires a switch between the replicative DNA polymerase (Pol) and a more specialized translesion synthesis (TLS) Pol to overcome the obstacle. DNA Pol delta-interacting protein 2 (PolDIP2) has been found to physically interact with Pol eta, Pol zeta, and Rev1, suggesting a possible role of PolDIP2 in the TLS reaction. However, the consequences of PolDIP2 interaction on the properties of TLS Pols remain unknown. Here, we analyzed the effects of PolDIP2 on normal and TLS by five different human specialized Pols from three families: Pol delta (family B), Pol eta and Pol iota (family Y), and Pol lambda and Pol beta (family X). Our results show that PolDIP2 also physically interacts with Pol lambda, which is involved in the correct bypass of 8-oxo-7,8-dihydroguanine (8-oxo-G) lesions. This interaction increases both the processivity and catalytic efficiency of the error-free bypass of a 8-oxo-G lesion by both Pols eta and lambda, but not by Pols beta or iota. Additionally, we provide evidence that PolDIP2 stimulates Pol delta without affecting its fidelity, facilitating the switch from Pol delta to Pol lambda during 8-oxo-G TLS. PolDIP2 stimulates Pols lambda and eta mediated bypass of other common DNA lesions, such as abasic sites and cyclobutane thymine dimers. Finally, PolDIP2 silencing increases cell sensitivity to oxidative stress and its effect is further potentiated in a Pol lambda deficient background, suggesting that PolDIP2 is an important mediator for TLS. |
