Structural insight into the substrate specificity of DNA Polymerase μ-Reference-Cited by-同舟云学术

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Structural insight into the substrate specificity of DNA Polymerase μ

Published:2006-12-10 Issue:1 Volume:14 Page:45-53
ISSN:1545-9993
Container-title:Nature Structural & Molecular Biology
language:en
Short-container-title:Nat Struct Mol Biol

Author:

Moon Andrea F,Garcia-Diaz Miguel,Bebenek Katarzyna,Davis Bryan J,Zhong Xuejun,Ramsden Dale A,Kunkel Thomas A,Pedersen Lars C

Publisher

Springer Science and Business Media LLC

Subject

Molecular Biology,Structural Biology

Link

http://www.nature.com/articles/nsmb1180.pdf

Reference46 articles.

1. Bebenek, K. & Kunkel, T.A. Functions of DNA polymerases. Adv. Protein Chem. 69, 137–165 (2004).

2. Braithwaite, E.K. et al. DNA polymerase lambda mediates a back-up base excision repair activity in extracts of mouse embryonic fibroblasts. J. Biol. Chem. 280, 18469–18475 (2005).

3. Garcia-Diaz, M., Bebenek, K., Kunkel, T.A. & Blanco, L. Identification of an intrinsic 5′-deoxyribose-5-phosphate lyase activity in human DNA polymerase lambda: a possible role in base excision repair. J. Biol. Chem. 276, 34659–34663 (2001).

4. Fan, W. & Wu, X. DNA polymerase lambda can elongate on DNA substrates mimicking non-homologous end joining and interact with XRCC4-ligase IV complex. Biochem. Biophys. Res. Commun. 323, 1328–1333 (2004).

5. Lee, J.W. et al. Implication of DNA polymerase lambda in alignment-based gap filling for nonhomologous DNA end joining in human nuclear extracts. J. Biol. Chem. 279, 805–811 (2004).

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