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• W2097188105 abstract "DNA polymerase λ (pol λ) 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 λ 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 λ 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 λ; (iii) pol λ preferentially generated G:T and G:G mismatches; (iv) RP-A, but not PCNA, selectively prevented misincorporation of an incorrect nucleotide by pol λ, without affecting correct incorporation and (v) this inhibitory effect required a precise ratio between the concentrations of pol λ and RP-A. Possible physiological implications of these findings for the in vivo fidelity of pol λ are discussed." @default.
• W2097188105 created "2016-06-24" @default.
• W2097188105 creator A5043762733 @default.
• W2097188105 date "2006-03-06" @default.
• W2097188105 modified "2023-10-18" @default.
• W2097188105 title "Human replication protein A can suppress the intrinsic in vitro mutator phenotype of human DNA polymerase " @default.
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• W2097188105 doi "https://doi.org/10.1093/nar/gkl032" @default.
• W2097188105 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/1390690" @default.
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