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Nucleic Acids Research 2006 34(5):1405-1415; doi:10.1093/nar/gkl032
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Published online 6 March 2006

© The Author 2006. 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@oxfordjournals.org

Article

Human replication protein A can suppress the intrinsic in vitro mutator phenotype of human DNA polymerase {lambda}

Giovanni Maga1,2,*, Igor Shevelev2, Giuseppe Villani3, Silvio Spadari1 and Ulrich Hübscher2

1Istituto di Genetica Molecolare IGM-CNR Pavia, Italy 2Institute of Veterinary Biochemistry and Molecular Biology, University of Zurich-Irchel Zurich, Switzerland 3Institut de Pharmacologie et de Biologie Structurale, IPBS-CNRS, Centre National de la Recherche Scientifique Toulouse, France

*To whom correspondence should be addressed at via Abbiategrasso 207, I-27100 Pavia, Italy. Tel: +39 038 254 6354; Fax: +39 038 242 2286; E-mail: maga{at}igm.cnr.it

Received January 3, 2006. Revised January 31, 2006. Accepted February 20, 2006.

DNA polymerase {lambda} (pol {lambda}) is a member of the X family DNA polymerases and is endowed with multiple enzymatic activities. In this work we investigated the in vitro miscoding properties of full-length, human pol {lambda} either in the absence or in the presence of the human auxiliary proteins proliferating cell nuclear antigen (PCNA) and replication protein A (RP-A). Our data suggested that (i) pol {lambda} had an intrinsic ability to create mismatches and to incorporate ribonucleotides at nearly physiological Mn++ and Mg++ concentrations; (ii) the sequence of the template-primer could influence the misincorporation frequency of pol {lambda}; (iii) pol {lambda} preferentially generated G:T and G:G mismatches; (iv) RP-A, but not PCNA, selectively prevented misincorporation of an incorrect nucleotide by pol {lambda}, without affecting correct incorporation and (v) this inhibitory effect required a precise ratio between the concentrations of pol {lambda} and RP-A. Possible physiological implications of these findings for the in vivo fidelity of pol {lambda} are discussed.


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