Permanent URL to this publication: http://dx.doi.org/10.5167/uzh-772
Maga, G; Shevelev, I V; Villani, G; Spadari, S; Hübscher, U (2006). Human replication protein A can suppress the intrinsic in vitro mutator phenotype of human DNA polymerase lambda. Nucleic Acids Research, 34(5):1405-1415.
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.
|Item Type:||Journal Article, refereed|
|Communities & Collections:||05 Vetsuisse Faculty > Institute of Veterinary Biochemistry and Molecular Biology|
|DDC:||570 Life sciences; biology|
|Date:||06 March 2006|
|Deposited On:||11 Feb 2008 13:18|
|Last Modified:||23 Nov 2012 16:59|
|Publisher:||Oxford University Press|
|WoS Citation Count:||19|
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