Results 1 to 10 of about 2,001 (190)
POLYNUCLEOTIDE LIGASE IN BACTERIOPHAGE T4D RECOMBINATION [PDF]
Genetics, 1972 ABSTRACT Following infection of E. coli B with ligase-deficient rII bacteriophage T4D recombination between linked markers is increased 4.2 fold and heterozygote frequency increased 2.3 fold. In such infection recombination occurs at a rapid rate for an extended period.
Henry Krisch +2 more
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Studies on Polynucleotides, C A Novel Joining Reaction Catalyzed by the T4-Polynucleotide Ligase [PDF]
Proceedings of the National Academy of Sciences, 1970 The polynucleotide ligase isolated from T4-infected Escherichia coli was previously shown to bring about repair of breaks in the single strands of bihelical DNA. The present work shows that the enzyme can also catalyze the joining of DNA duplexes at their base-paired ends.
V. Sgaramella +2 more
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Characterization of a Baculovirus Enzyme with RNA Ligase, Polynucleotide 5′-Kinase, and Polynucleotide 3′-Phosphatase Activities [PDF]
Journal of Biological Chemistry, 2004 The end-healing and end-sealing steps of the phage T4-induced RNA restriction-repair pathway are performed by two separate enzymes, a bifunctional polynucleotide 5'-kinase/3'-phosphatase and an ATP-dependent RNA ligase. Here we show that a single trifunctional baculovirus enzyme, RNA ligase 1 (Rnl1), catalyzes the identical set of RNA repair reactions.
Alexandra Martins, Stewart Shuman
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A Mutant of Bacteriophage T7 Deficient in Polynucleotide Ligase
Journal of Biological Chemistry, 1971 Abstract An amber mutant of bacteriophage T7, obtained by mutagenesis with hydroxylamine, fails to induce the T7 polynucleotide ligase upon infection of Escherichia coli. The mutant (T7amHA13) grows normally on a suppressor-negative host; its sensitivity to ultraviolet light is the same as that of wild type T7.
Yukito Masamune +2 more
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Kinetics and Effect of Salts and Polyamines on T4 Polynucleotide Ligase [PDF]
European Journal of Biochemistry, 1975 The kinetics of T4 polynucleotide ligase has been investigated at pH 8, 20 °C and using the double‐stranded DNA substrate (dA)n [(dT)10]n/10. Double‐reciprocal plots of initial rates vs substrate concentrations as well as product inhibition studies have indicated that the enzyme reacts according to a ping‐pong mechanism. The overall mechanism was found
Arnt J. Raae +2 more
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DNA replication in vivo by a temperature-sensitive polynucleotide ligase mutant of T4. [PDF]
Proceedings of the National Academy of Sciences, 1968 DNA replication in vivo as function of temperature sensitive polynucleotide ligase mutant Th, tsA80 in strand ...
Junko Hosoda, Eleanor Mathews
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Polynucleotide Ligase Activity of Eukaryotic Topoisomerase I [PDF]
Molecular Cell, 1998 Introduction of a single ribonucleoside immediately 5' of the scissile phosphate of a duplex DNA substrate converts eukaryotic topoisomerase I into an endoribonuclease. Here, I demonstrate that the RNase reaction is reversible. Vaccinia topoisomerase can ligate 2', 3'-cyclic phosphate and 5'-hydroxyl termini annealed to a bridging template strand ...
Stewart Shuman
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Repair of Alkylated Bacteriophage T4 Deoxyribonucleic Acid by a Mechanism Involving Polynucleotide Ligase [PDF]
Journal of Virology, 1971 Methyl methanesulfate-induced lesions in bacteriophage T4 are repaired primarily by a mechanism involving polynucleotide ligase. Apparently, other recombinational and ultraviolet repair functions aren't involved.
Marian W. Baldy +2 more
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Role of the DNA ligase III zinc finger in polynucleotide binding and ligation [PDF]
Nucleic Acids Research, 1998 Mammalian DNA ligase III exists as two distinct isoforms denoted alpha and beta. Both forms possess a motif that is homologous to the putative zinc finger present in poly(ADP-ribose) polymerase. Here, the role of this motif in the binding and ligation of nicked DNA and RNA substrates in vitro has been examined in both isoforms.
Rachel L. Taylor
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Polynucleotide 3′-terminal Phosphate Modifications by RNA and DNA Ligases [PDF]
Journal of Biological Chemistry, 2014 RNA and DNA ligases catalyze the formation of a phosphodiester bond between the 5'-phosphate and 3'-hydroxyl ends of nucleic acids. In this work, we describe the ability of the thermophilic RNA ligase MthRnl from Methanobacterium thermoautotrophicum to recognize and modify the 3'-terminal phosphate of RNA and single-stranded DNA (ssDNA).
Alexander Zhelkovsky, Larry McReynolds
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