Uncapping of viral messenger RNA by phosphodiesterase of fibroblast plasma membranes.
Isolated plasma membranes from mouse fibroblast lines 3T3 and its tranformant SV-3T3 contain a phosphodiesterase (oligonucleotidase, E.C. 3.1.4.19; nucleotide pyrophosphatase, E.C. 3.6.1.9) that splits capped and methylated messenger RNA obtained from both reovirus and vesicular stomatitis virus. The isolated membranes are free of demonstrable ribonuclease activity and split the mRNA to produce 7-methyl guanosine diphosphate as a product. With ATP as substrate for the phosphodiesterase enzyme, the product is AMP. Synthetic caps, AMP, ADP and ATP, but not cyclic AMP, can compete with the substrate p-nitrophenyl thymidilic acid. A possible regulatory role on messenger translation is proposed.
D000818:Animals; D002460:Cell Line; D002462:Cell Membrane / Q000201:enzymology; D002472:Cell Transformation, Viral; D051379:Mice; D010727:Phosphoric Diester Hydrolases / Q000378:metabolism*; D012333:RNA, Messenger / Q000378:metabolism*; D012367:RNA, Viral / Q000378:metabolism*; D012087:Reoviridae
D012333:RNA, Messenger; D012367:RNA, Viral; D010727:Phosphoric Diester Hydrolases