Site-Specific Ribonuclease Activity of Eukaryotic DNA Topoisomerase I
Identifieur interne : 003D22 ( Main/Exploration ); précédent : 003D21; suivant : 003D23Site-Specific Ribonuclease Activity of Eukaryotic DNA Topoisomerase I
Auteurs : Joann Sekiguchi [États-Unis] ; Stewart Shuman [États-Unis]Source :
- Molecular Cell [ 1097-2765 ] ; 1997.
English descriptors
- Teeft :
- Active site tyrosine, Adduct, Alkaline phosphatase, Biol, Ccctt, Chem, Cleavage, Cleavage product, Cleavage products, Cleavage reaction, Cleavage site, Covalent, Covalent adduct, Covalent adduct formation, Covalently, Cyclic, Cyclic phosphate, Denaturing polyacrylamide, Duplex, Enzyme, Ethanol, Ethanol precipitation, Eukaryotic, Eukaryotic type, Fmol, Free cleavage product, Human topoisomerase, Ligation, Molecular cell, Nucleic, Nucleic acid, Nucleic acids, Nucleotide, Petersen, Phosphatase, Phosphodiester, Pmol, Polyacrylamide, Precipitation, Reaction mixture, Reaction mixtures, Reaction products, Religation, Ribonuclease, Ribonuclease activity, Ribonucleoside, Ribonucleotides, Ribose sugar, Rnase, Rnase activity, Scissile, Scissile phosphate, Scissile phosphodiester, Scissile ribonucleotide, Scissile strand, Sekiguchi, Shuman, Single ribonucleoside, Single ribouridine substitution, Strand, Strand cleavage, Strand scission, Strand transfer reactions, Suicide substrate, Topoisomerase, Topoisomerase cleavage, Topoisomerase cleavage product, Topoisomerases, Transesterification, Transesterification reaction, Trna, Vaccinia, Vaccinia topoisomerase, Vaccinia virus, Westergaard.
Abstract
Abstract: Type I topoisomerases alter DNA topology by cleaving and rejoining one strand of duplex DNA through a covalent protein–DNA intermediate. Here we show that vaccinia topoisomerase, a eukaryotic type IB enzyme, catalyzes site-specific endoribonucleolytic cleavage of an RNA-containing strand. The RNase reaction occurs via transesterification at the scissile ribonucleotide to form a covalent RNA-3′-phosphoryl-enzyme intermediate, which is then attacked by the vicinal 2′ OH of the ribose sugar to yield a free 2′, 3′ cyclic phosphate product. Introduction of a single ribonucleoside at the scissile phosphate of an otherwise all-DNA substrate suffices to convert the topoisomerase into an endonuclease. Human topoisomerase I also has endoribonuclease activity. These findings suggest potential roles for topoisomerases in RNA processing.
Url:
DOI: 10.1016/S1097-2765(00)80010-6
Affiliations:
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acids</term><term>Nucleotide</term><term>Petersen</term><term>Phosphatase</term><term>Phosphodiester</term><term>Pmol</term><term>Polyacrylamide</term><term>Precipitation</term><term>Reaction mixture</term><term>Reaction mixtures</term><term>Reaction products</term><term>Religation</term><term>Ribonuclease</term><term>Ribonuclease activity</term><term>Ribonucleoside</term><term>Ribonucleotides</term><term>Ribose sugar</term><term>Rnase</term><term>Rnase activity</term><term>Scissile</term><term>Scissile phosphate</term><term>Scissile phosphodiester</term><term>Scissile ribonucleotide</term><term>Scissile strand</term><term>Sekiguchi</term><term>Shuman</term><term>Single ribonucleoside</term><term>Single ribouridine substitution</term><term>Strand</term><term>Strand cleavage</term><term>Strand scission</term><term>Strand transfer reactions</term><term>Suicide substrate</term><term>Topoisomerase</term><term>Topoisomerase cleavage</term><term>Topoisomerase cleavage 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Here we show that vaccinia topoisomerase, a eukaryotic type IB enzyme, catalyzes site-specific endoribonucleolytic cleavage of an RNA-containing strand. The RNase reaction occurs via transesterification at the scissile ribonucleotide to form a covalent RNA-3′-phosphoryl-enzyme intermediate, which is then attacked by the vicinal 2′ OH of the ribose sugar to yield a free 2′, 3′ cyclic phosphate product. Introduction of a single ribonucleoside at the scissile phosphate of an otherwise all-DNA substrate suffices to convert the topoisomerase into an endonuclease. Human topoisomerase I also has endoribonuclease activity. 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