Results 1 to 10 of about 70 (70)

POLYNUCLEOTIDE LIGASE IN BACTERIOPHAGE T4D RECOMBINATION [PDF]

open access: yesGenetics, 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.
H M, Krisch, N V, Hamlett, H, Berger
openaire   +2 more sources

Studies on Polynucleotides, C A Novel Joining Reaction Catalyzed by the T4-Polynucleotide Ligase [PDF]

open access: yesProceedings 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
openaire   +2 more sources

Monitoring regulation of DNA repair activities of cultured cells in-gel using the comet assay

open access: yesFrontiers in Genetics, 2014
Base excision repair (BER) is the predominant cellular mechanism by which human cells repair DNA base damage, sites of base loss and DNA single strand breaks of various complexity, that are generated in their thousands in every human cell per day as a ...
Jason Luke Parsons   +1 more
doaj   +1 more source

Characterization of a Baculovirus Enzyme with RNA Ligase, Polynucleotide 5′-Kinase, and Polynucleotide 3′-Phosphatase Activities [PDF]

open access: yesJournal 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
openaire   +2 more sources

Polynucleotide Ligase Activity of Eukaryotic Topoisomerase I [PDF]

open access: yesMolecular 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 ...
openaire   +2 more sources

Polynucleotide 3′-terminal Phosphate Modifications by RNA and DNA Ligases [PDF]

open access: yesJournal 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 M, Zhelkovsky   +1 more
openaire   +2 more sources

A Mutant of Bacteriophage T7 Deficient in Polynucleotide Ligase

open access: yesJournal 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.
Y, Masamune   +2 more
openaire   +2 more sources

Purification and Properties of a Polynucleotide Ligase from Human Cell Cultures [PDF]

open access: yesEuropean Journal of Biochemistry, 1971
A polynucleotide ligase has been detected and purified over 300‐fold from human cells cultured in vitro. The enzymic activity is dependent on ATP and Mg2+. The pH curve is bimodal with two optima at pH 7.5 and 8.1. The purified enzyme requires for its activity a heat‐resistant protein factor present in the crude extract.
S, Spadari, G, Ciarrocchi, A, Falaschi
openaire   +2 more sources

Kinetics and Effect of Salts and Polyamines on T4 Polynucleotide Ligase [PDF]

open access: yesEuropean 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
A J, Raae, R K, Kleppe, K, Kleppe
openaire   +2 more sources

m5C‐Modified tRF3b‐CysGCA‐23 Suppresses Bladder Cancer Malignancy by Repressing H3K18 Lactylation via Stabilizing RBM4

open access: yesAdvanced Science, EarlyView.
In this study, we identified an NSUN6‐dependent m5C‐modified tsRNA, m5C‐tRF3b CysGCA‐23 (mtRC), that is downregulated in BC and inversely correlated with disease progression. Mechanistically, mtRC suppresses BC malignancy by stabilizing RBM4, attenuating glycolysis, and thereby limiting H3K18 lactylation–mediated activation of IL1RAP and VASH2 ...
Xiaoling Ying   +16 more
wiley   +1 more source

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