Results 151 to 160 of about 76,419 (179)
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Interdomain assembly between the fungal tRNA ligase adenylyltransferase and kinase domain.
RNA: A publication of the RNA SocietyTrl1-type ligases play an essential role in fungi and plants during the non-conventional tRNA splicing as well as the unfolded protein response. The tripartite enzyme consists of an N-terminal adenylyltransferase domain (LIG), a central polynucleotide ...
Sandra Köhler, Jirka Peschek
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The polynucleotide ligase and RNA capping enzyme superfamily of covalent nucleotidyltransferases
Current Opinion in Structural Biology, 2004ATP- and NAD(+)-dependent DNA ligases, ATP-dependent RNA ligases and GTP-dependent mRNA capping enzymes comprise a superfamily of proteins that catalyze nucleotidyl transfer to polynucleotide 5' ends via covalent enzyme-(lysyl-N)-NMP intermediates. The superfamily is defined by five peptide motifs that line the nucleotide-binding pocket and contribute ...
Christopher D. Lima, Stewart Shuman
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Changes in polynucleotide ligase during rat liver regeneration
Biochemical and Biophysical Research Communications, 1974Abstract The specific activity of polynucleotide ligase in rat liver seems to begin to rise at 16 hours after partial hepatectomy (removal of 70% of the liver). The increases reach their maxima about 24 hours after operation, rising to at least 4 to 5 fold normal levels.
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T4 polynucleotide ligase catalyzed joining on triple-stranded nucleic acids
Biochemistry, 1978dT1O will form triple-stranded complexes with dAn and these complexes can serve as substrate for T4 polynucleotide ligase (EC 6.5.1.1). The rate of phosphodiester formation was found to be approximately the same as for the double-stranded complex and, furthermore, the rate appears to be similar on the two strands in the complex.
Arnt J. Raae, Kjell Kleppe
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Biochemical and Biophysical Research Communications, 1970
Abstract The fidelity of phage T 4 -induced polynucleotide ligase has been studied by using chemically synthesized deoxyribooligonucleotide p 3 2 T 1 2 and p 3 2 T 1 1 C. In the presence of polydeoxyadenylate,each substrate is joined by ligase to form longer chain deoxyribopolynucleotides.
Tsiapalis, C., Narang, S.
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Abstract The fidelity of phage T 4 -induced polynucleotide ligase has been studied by using chemically synthesized deoxyribooligonucleotide p 3 2 T 1 2 and p 3 2 T 1 1 C. In the presence of polydeoxyadenylate,each substrate is joined by ligase to form longer chain deoxyribopolynucleotides.
Tsiapalis, C., Narang, S.
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Enzymic joining of polynucleotides
Journal of Molecular Biology, 1969Abstract After mixed infection of Escherichia coli strain BB with 32P-labeled- and bromouracil density-labeled T4 am EB6 (a T4 mutant defective in the DNA polymerase gene), two kinds of hybrid molecules were isolated. One type contained the 32P- and bromouracil-labeled components linked only by hydrogen bonds (joint molecules); the second type ...
I. R. Lehman, Naoyo Anraku
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Chemico-Biological Interactions, 1981
Conformationally distinct chromatin populations were utilized as substrates to quantitate the relative amount of and accessibility of internal 5'-phosphomonoester breaks in DNA-chromatin. In these studies, a constant amount of chromatin as well as deproteinized DNA derived from the respective chromatin sample was titrated with increasing quantities of ...
Frederick F. Becker +3 more
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Conformationally distinct chromatin populations were utilized as substrates to quantitate the relative amount of and accessibility of internal 5'-phosphomonoester breaks in DNA-chromatin. In these studies, a constant amount of chromatin as well as deproteinized DNA derived from the respective chromatin sample was titrated with increasing quantities of ...
Frederick F. Becker +3 more
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Journal of Molecular Biology, 1972
Abstract T4 polynucleotide ligase catalyzes the end-to-end joining of DNA duplexes at the base-paired ends. The reaction has been shown to be bi-molecular in character by using a mixture of two different duplexes, when covalent joining of the two duplexes was observed. The reaction showed a temperature optimum of 25 °C.
V. Sgaramella, H G Khorana
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Abstract T4 polynucleotide ligase catalyzes the end-to-end joining of DNA duplexes at the base-paired ends. The reaction has been shown to be bi-molecular in character by using a mixture of two different duplexes, when covalent joining of the two duplexes was observed. The reaction showed a temperature optimum of 25 °C.
V. Sgaramella, H G Khorana
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Role of polynucleotide ligase in T4 DNA replication
Journal of Molecular Biology, 1968Philip C. Hanawalt, Jean Newman
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