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http://purl.uniprot.org/citations/17005572http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/17005572http://www.w3.org/2000/01/rdf-schema#comment"During short-patch base excision repair, the excision of a 5'-terminal 2-deoxyribose-5-phosphate moiety of the downstream strand by the 5'-2-deoxyribose-5-phosphate lyase activity of either DNA polymerase beta or lambda is believed to occur after each respective enzyme catalyzes gap-filling DNA synthesis. Yet the effects of this 5'-terminal 2-deoxyribose-5-phosphate moiety on the polymerase activities of these two enzymes have never been quantitatively determined. Moreover, x-ray crystal structures of truncated polymerase lambda have revealed that the downstream strand and its 5'-phosphate group of gapped DNA interact intensely with the dRPase domain, but the kinetic effect of these interactions is unclear. Here, we utilized pre-steady state kinetic methods to systematically investigate the effect of a downstream strand and its 5'-moieties on the polymerase activity of the full-length human polymerase lambda. The downstream strand and its 5'-phosphate were both found to increase nucleotide incorporation efficiency (kp/Kd) by 15 and 11-fold, respectively, with the increase procured by the effect on the nucleotide incorporation rate constant kp rather than the ground state nucleotide binding affinity Kd. With 4 single nucleotide-gapped DNA substrates containing a 1,2-dideoxyribose-5-phosphate moiety, a 2-deoxyribose-5-phosphate mimic, we measured the incorporation efficiencies of 16 possible nucleotides. Our results demonstrate that although this 5'-terminal 2-deoxyribose-5-phosphate mimic does not affect the fidelity of polymerase lambda, it moderately decreased the polymerase efficiency by 3.4-fold. Moreover, this decrease in polymerase efficiency is due to a drop of similar magnitude in kp rather than Kd. The implication of the downstream strand and its 5'-moieties on the kinetics of gap-filling synthesis is discussed."xsd:string
http://purl.uniprot.org/citations/17005572http://purl.org/dc/terms/identifier"doi:10.1074/jbc.m607479200"xsd:string
http://purl.uniprot.org/citations/17005572http://purl.uniprot.org/core/author"Suo Z."xsd:string
http://purl.uniprot.org/citations/17005572http://purl.uniprot.org/core/author"Bhatt N."xsd:string
http://purl.uniprot.org/citations/17005572http://purl.uniprot.org/core/author"Fiala K.A."xsd:string
http://purl.uniprot.org/citations/17005572http://purl.uniprot.org/core/author"Duym W.W."xsd:string
http://purl.uniprot.org/citations/17005572http://purl.uniprot.org/core/date"2006"xsd:gYear
http://purl.uniprot.org/citations/17005572http://purl.uniprot.org/core/name"J Biol Chem"xsd:string
http://purl.uniprot.org/citations/17005572http://purl.uniprot.org/core/pages"35649-35655"xsd:string
http://purl.uniprot.org/citations/17005572http://purl.uniprot.org/core/title"Kinetic effect of a downstream strand and its 5'-terminal moieties on single nucleotide gap-filling synthesis catalyzed by human DNA polymerase lambda."xsd:string
http://purl.uniprot.org/citations/17005572http://purl.uniprot.org/core/volume"281"xsd:string
http://purl.uniprot.org/citations/17005572http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/17005572
http://purl.uniprot.org/citations/17005572http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/17005572
http://purl.uniprot.org/uniprot/#_B7Z1M4-mappedCitation-17005572http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/17005572
http://purl.uniprot.org/uniprot/#_B3KXT3-mappedCitation-17005572http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/17005572
http://purl.uniprot.org/uniprot/#_B4DE17-mappedCitation-17005572http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/17005572
http://purl.uniprot.org/uniprot/#_B4DUZ9-mappedCitation-17005572http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/17005572
http://purl.uniprot.org/uniprot/#_A8K860-mappedCitation-17005572http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/17005572
http://purl.uniprot.org/uniprot/#_B4DEF5-mappedCitation-17005572http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/17005572
http://purl.uniprot.org/uniprot/#_Q5JQP8-mappedCitation-17005572http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/17005572
http://purl.uniprot.org/uniprot/#_Q5QJV5-mappedCitation-17005572http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/17005572
http://purl.uniprot.org/uniprot/#_Q5ZEY5-mappedCitation-17005572http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/17005572
http://purl.uniprot.org/uniprot/#_Q5ZEY6-mappedCitation-17005572http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/17005572
http://purl.uniprot.org/uniprot/#_Q9HBN3-mappedCitation-17005572http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/17005572