Site-specific ribonuclease activity of eukaryotic DNA topoisomerase I Journal Article


Authors: Sekiguchi, J.; Shuman, S.
Article Title: Site-specific ribonuclease activity of eukaryotic DNA topoisomerase I
Abstract: Type I topoisomerases alter DN A 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-DMA 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.
Keywords: genetics; molecular genetics; metabolism; enzymology; tyrosine; physiology; dna; molecular sequence data; kinetics; messenger rna; rna, messenger; nucleotide sequence; substrate specificity; vaccinia virus; base sequence; eukaryotic cell; enzyme specificity; phosphate; phosphates; uridine; ribonucleases; thymidine; dna topoisomerase; dna topoisomerases, type i; ribonuclease; eukaryotic cells; humans; human; article
Journal Title: Molecular Cell
Volume: 1
Issue: 1
ISSN: 1097-2765
Publisher: Cell Press  
Date Published: 1997-12-01
Start Page: 89
End Page: 97
Language: English
PUBMED: 9659906
PROVIDER: scopus
DOI: 10.1016/S1097-2765(00)80010-6
DOI/URL:
Notes: Article -- Export Date: 17 March 2017 -- Source: Scopus
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  1. Stewart H Shuman
    546 Shuman