ArticleNucleic acids research2003
Mutagenesis of human DNA polymerase lambda: essential roles of Tyr505 and Phe506 for both DNA polymerase and terminal transferase activities.
Article in Nucleic acids research, 2003. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 16 papers.
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16 citing papers in PubMed, 24 citations in OpenAlex.
- Time-lapse crystallography snapshots of a double-strand break repair polymerase in action.Nature communications · 2017Article
- Gap-directed translesion DNA synthesis of an abasic site on circular DNA templates by a human replication complex.PloS one · 2014Article
- A specific N-terminal extension of the 8 kDa domain is required for DNA end-bridging by human Polμ and Polλ.Nucleic acids research · 2013Article
- In vitro gap-directed translesion DNA synthesis of an abasic site involving human DNA polymerases epsilon, lambda, and beta.The Journal of biological chemistry · 2011Article
- Interaction between DNA Polymerase lambda and anticancer nucleoside analogs.The Journal of biological chemistry · 2010Article
- DNA polymerase family X: function, structure, and cellular roles.Biochimica et biophysica acta · 2010Review
- Conferring a template-dependent polymerase activity to terminal deoxynucleotidyltransferase by mutations in the Loop1 region.Nucleic acids research · 2009Article
- Catalytic mechanism of human DNA polymerase lambda with Mg2+ and Mn2+ from ab initio quantum mechanical/molecular mechanical studies.DNA repair · 2008Article
- Editing of misaligned 3'-termini by an intrinsic 3'-5' exonuclease activity residing in the PHP domain of a family X DNA polymerase.Nucleic acids research · 2008Article
- The X family portrait: structural insights into biological functions of X family polymerases.DNA repair · 2007Review
- Error-free bypass of 2-hydroxyadenine by human DNA polymerase lambda with Proliferating Cell Nuclear Antigen and Replication Protein A in different sequence contexts.Nucleic acids research · 2007Article
- Expanding the repertoire of DNA polymerase substrates: template-instructed incorporation of non-nucleoside triphosphate analogues by DNA polymerases beta and lambda.Nucleic acids research · 2007Article
- Sequential side-chain residue motions transform the binary into the ternary state of DNA polymerase lambda.Biophysical journal · 2006Article
- Human replication protein A can suppress the intrinsic in vitro mutator phenotype of human DNA polymerase lambda.Nucleic acids research · 2006Article
- Inhibition of mammalian DNA polymerases by resveratrol: mechanism and structural determinants.The Biochemical journal · 2005Article
- Incorporation of non-nucleoside triphosphate analogues opposite to an abasic site by human DNA polymerases beta and lambda.Nucleic acids research · 2005Article
Corrections and comments
- Erratum issued
Authors and funding
7 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
DNA polymerase (pol) lambda is homologous to pol beta and has intrinsic polymerase and terminal transferase activities. However, nothing is known about the amino acid residues involved in these activities. In order to precisely define the nucleotide-binding site of human pol lambda, we have mutagenised two amino acids, Tyr505 and the neighbouring Phe506, which were predicted by structural homology modelling to correspond to the Tyr271 and Phe272 residues of pol beta, which are involved in nucleotide binding. Our analysis demonstrated that pol lambda Phe506Arg/Gly mutants possess very low polymerase and terminal transferase activities as well as greatly reduced abilities for processive DNA synthesis and for carrying on translesion synthesis past an abasic site. The Tyr505Ala mutant, on the other hand, showed an altered nucleotide binding selectivity to perform the terminal transferase activity. Our results suggest the existence of a common nucleotide-binding site for the polymerase and terminal transferase activities of pol lambda, as well as distinct roles of the amino acids Tyr505 and Phe506 in these two catalytic functions.
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