A structural solution for the DNA polymerase lambda-dependent repair of DNA gaps with minimal homology |
| |
Authors: | Garcia-Diaz Miguel Bebenek Katarzyna Krahn Joseph M Blanco Luis Kunkel Thomas A Pedersen Lars C |
| |
Institution: | Laboratory of Molecular Genetics, National Institute of Environmental Health Sciences, Research Triangle Park, NC 27709, USA. |
| |
Abstract: | Human DNA polymerase lambda (Pol lambda) is a family X member with low frameshift fidelity that has been suggested to perform gap-filling DNA synthesis during base excision repair and during repair of broken ends with limited homology. Here, we present a 2.1 A crystal structure of the catalytic core of Pol lambda in complex with DNA containing a two nucleotide gap. Pol lambda makes limited contacts with the template strand at the polymerase active site, and superimposition with Pol beta in a ternary complex suggests a shift in the position of the DNA at the active site that is reminiscent of a deletion intermediate. Surprisingly, Pol lambda can adopt a closed conformation, even in the absence of dNTP binding. These observations have implications for the catalytic mechanism and putative DNA repair functions of Pol lambda. |
| |
Keywords: | |
本文献已被 PubMed 等数据库收录! |
|