| Article ID | Journal | Published Year | Pages | File Type |
|---|---|---|---|---|
| 8320778 | DNA Repair | 2014 | 12 Pages |
Abstract
- The Polλ BRCT domain increases the efficiency of abasic site bypass.
- The Polλ proline-rich domain stimulates generation of â2 frameshift mutations.
- The Polλ BRCT domain represses spontaneous generation of â2 frameshift mutations.
- The N-terminal domains of Polλ cooperatively promote looping out of damaged bases.
Keywords
BRCTdRPasePCNA2′-deoxynucleoside 5′-triphosphate8-oxodGBRCA1 C-terminal domaindNTPBERPAGENHEJTLS8-oxo-7,8-dihydro-2′-deoxyguanosineapurinic/apyrimidinicBSAPolβbovine serum albuminProliferating Cell Nuclear Antigenpolyacrylamide gel electrophoresisbase excision repairabasic sitetranslesion DNA synthesislesion bypassNonhomologous end joining
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Authors
David J. Taggart, Daniel M. Dayeh, Saul W. Fredrickson, Zucai Suo,