An enzyme which specifically splits a covalent bond between picornaviral RNA and VPg.
An enzyme which specifically splits a covalent bond between VPg and picornaviral RNAs (tentatively designated Y-pUpN PDE) has been partially purified from mouse ascites Krebs II cells. Using substrates labelled in vitro with 125I-Bolton-Hunter reagent and a new assay based on Kieselgel thin-layer chromatography, several biochemical characteristics of the enzyme have been determined, depending on the pH and on Mg2+, K+, spermidine and PEG concentrations, etc. We found that the enzyme does not 'unlink' VPg from comoviral RNA. We suggest that Y-pUpN PDE represents a new class of enzymes.
Drygin YuF
A.N. Belozersky Laboratory of Molecular Biology and Bioorganic Chemistry, Moscow State University, USSR.
Shabanov
A A
AA
Bogdanov
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AA
D000818:Animals; D002287:Carcinoma, Krebs 2 / Q000201:enzymology; D051379:Mice; D010727:Phosphoric Diester Hydrolases / Q000378:metabolism*; D010849:Picornaviridae / Q000378:metabolism*; D012367:RNA, Viral / Q000378:metabolism*; D014758:Viral Core Proteins / Q000378:metabolism*
D012367:RNA, Viral; D014758:Viral Core Proteins; D010727:Phosphoric Diester Hydrolases; C025672:RNA-tyrosine phosphatase