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Nucleic Acids Research 2005 33(16):5354-5361; doi:10.1093/nar/gki845
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Published online 20 September 2005

© The Author 2005. Published by Oxford University Press. All rights reserved
The online version of this article has been published under an open access model. Users are entitled to use, reproduce, disseminate, or display the open access version of this article for non-commercial purposes provided that: the original authorship is properly and fully attributed; the Journal and Oxford University Press are attributed as the original place of publication with the correct citation details given; if an article is subsequently reproduced or disseminated not in its entirety but only in part or as a derivative work this must be clearly indicated. For commercial re-use, please contact journals.permissions{at}oxfordjournals.org

Article

Phosphorylation of human DNA polymerase {lambda} by the cyclin-dependent kinase Cdk2/cyclin A complex is modulated by its association with proliferating cell nuclear antigen

Isabelle Frouin, Magali Toueille, Elena Ferrari, Igor Shevelev and Ulrich Hübscher*

Institute of Veterinary Biochemistry and Molecular Biology, University of Zürich-Irchel Winterthurerstrasse 190, CH-8057 Zürich, Switzerland

*To whom correspondence should be addressed. Tel: + 41 16 35 54 72/71; Fax: +41 16 35 68 40; Email: hubscher{at}vetbio.unizh.ch

Received August 16, 2005. Revised August 31, 2005. Accepted August 31, 2005.

DNA polymerase (Pol) {lambda} is a member of the Pol X family and possesses four different enzymatic activities, being DNA polymerase, terminal transferase, deoxyribose phosphate lyase and polynucleotide synthetase, all localized in its C-terminal region. On the basis of its biochemical properties, Pol {lambda} has been implicated in various DNA repair pathways, such as abasic site translesion DNA synthesis, base excision repair and non-homologous end joining of double strand breaks. However, its role in vivo has not yet been elucidated. In addition, Pol {lambda} has been shown to interact with the replication clamp proliferating cell nuclear antigen (PCNA) in vitro and in vivo. In this work, we searched by affinity chromatography for novel partners and we identified the cyclin-dependent kinase Cdk2 as novel partner of Pol {lambda}. Pol {lambda} is phosphorylated in vitro by several Cdk/cyclin complexes, including Cdk2/cyclin A, in its proline-serine-rich domain. While the polymerase activity of Pol {lambda} was not affected by Cdk2/cyclin A phosphorylation, phosphorylation of Pol {lambda} was decreased by its interaction with PCNA. Finally, Pol {lambda} is also phosphorylated in vivo in human cells and this phosphorylation is modulated during the cell cycle.


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