NDLI: In Vitro Gap-directed Translesion DNA Synthesis of an Abasic Site Involving Human DNA Polymerases ϵ, λ, and β

Content Provider	Journal of Biological Chemistry (JBC)
Author	Villani, Giuseppe Hubscher, Ulrich Gironis, Nadege Parkkinen, Sinikka Pospiech, Helmut Shevelev, Igor Cicco, Giulia Di Markkanen, Enni Syväoja, Juhani E. Gac, Nicolas Tanguy Le
Abstract	DNA polymerase (pol) ϵ is thought to be the leading strand replicase in eukaryotes, whereas pols λ and β are believed to be mainly involved in re-synthesis steps of DNA repair. DNA elongation by the human pol ϵ is halted by an abasic site (apurinic/apyrimidinic (AP) site). In this study, we present in vitro evidence that human pols λ, β, and η can perform translesion synthesis (TLS) of an AP site in the presence of pol ϵ, likely by initiating the 3′OHs created at the lesion by the arrested pol ϵ. However, in the case of pols λ and β, this TLS requires the presence of a DNA gap downstream from the product synthesized by the pol ϵ, and the optimal gap for efficient TLS is different for the two polymerases. The presence of gaps did not affect the TLS capacity of human pol η. Characterization of the reaction products showed that pol β inserted dAMP opposite the AP site, whereas gap filling synthesis by pol λ resulted in single or double deletions opposite the lesion. The synthesis up to the AP site by pol ϵ and the subsequent TLS by pols λ and β are not influenced by human processivity factor proliferating cell nuclear antigen and human single-stranded DNA-binding protein replication protein A. The bypass capacity of pol λ at the AP site is greatly reduced when a truncated form of the enzyme, which has lost the BRCA1 C-terminal and proline-rich domains, is used. Collectively, our in vitro results support the existence of a mechanism of gap-directed TLS at an AP site involving a switch between the replicative pol ϵ and the repair pols λ and β.
Related Links	http://www.jbc.org/content/286/37/32094.abstract
Ending Page	32104
Starting Page	32094
Page Count	11
File Format	HTM / HTML PDF
ISSN	00219258
Journal	Journal of Biological Chemistry (JBC)
Issue Number	37
Volume Number	286
DOI	10.1074/jbc.M111.246611
e-ISSN	1083351X
Language	English
Publisher	American Society for Biochemistry and Molecular Biology
Publisher Date	2011-09-16
Access Restriction	Open
Subject Keyword	DNA Damage DNA Polymerase DNA Repair DNA Replication DNA-Protein Interaction DNA and Chromosomes
Content Type	Text
Resource Type	Article
Subject	Cell Biology Biochemistry Molecular Biology

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