Abstract
The major DNA ligase of proliferating mammalian cells, DNA ligase I, catalyzes the joining of single strand breaks in double stranded DNA and is active on a synthetic substrate of oligo(dT) hybridized to poly(dA). DNA ligase I does not catalyze the joining of an oligo(dT).poly(rA) substrate. Two additional DNA ligases, II and III, which can act on the latter substrate have been purified from calf thymus. DNA ligase II, which has been described previously, is a 72-kDa protein. DNA ligase III migrates as a 100-kDa protein in denaturing gel electrophoresis. Structural, immunochemical, and catalytic studies on the three DNA ligase activities strongly indicate that they are the products of three different genes.
MeSH terms
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Adenosine Monophosphate / metabolism
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Adenosine Triphosphate / metabolism
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Amino Acid Sequence
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Animals
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Cattle
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Chromatography, Gel
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Chromatography, High Pressure Liquid
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Chromatography, Ion Exchange
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DNA Ligase ATP
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DNA Ligases / genetics
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DNA Ligases / isolation & purification*
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DNA Ligases / metabolism
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Electrophoresis, Polyacrylamide Gel
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Immune Sera
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Immunoblotting
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Kinetics
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Molecular Sequence Data
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Molecular Weight
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Peptide Mapping
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Peptides / chemical synthesis
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Peptides / immunology
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Poly-ADP-Ribose Binding Proteins
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Thymus Gland / enzymology*
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Xenopus Proteins
Substances
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Immune Sera
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Peptides
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Poly-ADP-Ribose Binding Proteins
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Xenopus Proteins
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Adenosine Monophosphate
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Adenosine Triphosphate
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DNA Ligases
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DNA Ligase ATP
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DNA ligase III alpha protein, Xenopus