ArticleNucleic acids research1998
Chlorella virus DNA ligase: nick recognition and mutational analysis.
Article in Nucleic acids research, 1998. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 32 papers.
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Who cites it
32 citing papers in PubMed, 80 citations in OpenAlex.
- Caveat mutator: alanine substitutions for conserved amino acids in RNA ligase elicit unexpected rearrangements of the active site for lysine adenylylation.Nucleic acids research · 2020Article
- Structural intermediates of a DNA-ligase complex illuminate the role of the catalytic metal ion and mechanism of phosphodiester bond formation.Nucleic acids research · 2019Article
- DNA binding with a minimal scaffold: structure-function analysis of Lig E DNA ligases.Nucleic acids research · 2018Article
- Structures of DNA-bound human ligase IV catalytic core reveal insights into substrate binding and catalysis.Nature communications · 2018Article
- The Sole DNA Ligase inFrontiers in cellular and infection microbiology · 2018Article
- The Inhibitory Effect of Non-Substrate and Substrate DNA on the Ligation and Self-Adenylylation Reactions Catalyzed by T4 DNA Ligase.PloS one · 2016Article
- Human DNA ligase III bridges two DNA ends to promote specific intermolecular DNA end joining.Nucleic acids research · 2015Article
- From Structure-Function Analyses to Protein Engineering for Practical Applications of DNA Ligase.Archaea (Vancouver, B.C.) · 2015Review
- Efficient DNA ligation in DNA-RNA hybrid helices by Chlorella virus DNA ligase.Nucleic acids research · 2014Article
- The sequential 2',3'-cyclic phosphodiesterase and 3'-phosphate/5'-OH ligation steps of the RtcB RNA splicing pathway are GTP-dependent.Nucleic acids research · 2012Article
- Kinetic analysis of DNA strand joining by Chlorella virus DNA ligase and the role of nucleotidyltransferase motif VI in ligase adenylylation.The Journal of biological chemistry · 2012Article
- Kinetic characterization of single strand break ligation in duplex DNA by T4 DNA ligase.The Journal of biological chemistry · 2011Article
- Structure-function analysis of the OB and latch domains of chlorella virus DNA ligase.The Journal of biological chemistry · 2011Article
- Functional dissection of the DNA interface of the nucleotidyltransferase domain of chlorella virus DNA ligase.The Journal of biological chemistry · 2011Article
- RNA 3'-phosphate cyclase (RtcA) catalyzes ligase-like adenylylation of DNA and RNA 5'-monophosphate ends.The Journal of biological chemistry · 2011Article
- Virtual high-throughput screening identifies mycophenolic acid as a novel RNA capping inhibitor.PloS one · 2011Article
- Template-directed ligation of tethered mononucleotides by t4 DNA ligase for kinase ribozyme selection.PloS one · 2010Article
- Profiling the selectivity of DNA ligases in an array format with mass spectrometry.Nucleic acids research · 2010Article
- Structure-activity relationships in human RNA 3'-phosphate cyclase.RNA (New York, N.Y.) · 2009Article
- Sequence-specific 1H N, 13C, and 15N backbone resonance assignments of the 34 kDa Paramecium bursaria Chlorella virus 1 (PBCV1) DNA ligase.Biomolecular NMR assignments · 2009Article
Corrections and comments
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Chlorella virus PBCV-1 DNA ligase seals nicked DNA substrates consisting of a 5'-phosphate-terminated strand and a 3'-hydroxyl-terminated strand annealed to a bridging DNA template strand. The enzyme discriminates at the DNA binding step between substrates containing a 5'-phosphate versus a 5'-hydroxyl at the nick. Mutational analysis of the active site motif KxDGxR (residues 27-32) illuminates essential roles for the conserved Lys, Asp and Arg moieties at different steps of the ligase reaction. Mutant K27A is unable to form the covalent ligase-(Lys-straightepsilonN-P)-adenylate intermediate and hence cannot activate a nicked DNA substrate via formation of the DNA-adenylate intermediate. Nonetheless, K27A catalyzes phosphodiester bond formation at a pre-adenylated nick. This shows that the active site lysine is not required for the strand closure reaction. K27A binds to nicked DNA-adenylate, but not to a standard DNA nick. This suggests that occupancy of the AMP binding pocket of DNA ligase is important for nick recognition. Mutant D29A is active in enzyme-adenylate formation and binds readily to nicked DNA, but is inert in DNA-adenylate formation. R32A is unable to catalyze any of the three reactions of the ligation pathway and does not bind to nicked DNA.
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