title: [RNA-protein interactions in influenza virus A ribonucleoprotein detected by UV radiation].
abstract: RNA and protein interaction in the structure of influenza virus ribonucleoprotein (RNP) was studied by ultraviolet (UV) irradiation. After UV-irradiation of virion RNP for 1 hour only 6% of 3H-uridine-labeled RNA was found to go into the aqueous phase upon phenol-detergent extraction. Pretreatment of RNP with small doses of pancreatic RNase before RNA extraction slightly increased (up to 18%) the amount of RNA going into the aqueous phase. About 90% RNA was found after extraction in the aqueous phase in the nonirradiated material. As a result of UV-irradiation of RNP, RNA in RNP became more resistant to RNase: the residual acid-insoluble radioactivity was 21% whereas with nonirradiated RNP it was 3.2%. The results of the analysis of RNP labeled for protein in polyacrylamide gel and SDS-sucrose gradient after UV-irradiation and ribonuclease treatment indicate the formation of UV-induced linkages between RNA and NP protein.
mesh_terms: D000818:Animals; D002642:Chick Embryo; D004347:Drug Interactions / Q000528:radiation effects; D004591:Electrophoresis, Polyacrylamide Gel; D009980:Influenza A virus / Q000032:analysis / Q000528:radiation effects*; D009698:Nucleoproteins / Q000528:radiation effects*; D012367:RNA, Viral / Q000032:analysis / Q000528:radiation effects*; D012261:Ribonucleoproteins / Q000032:analysis / Q000528:radiation effects*; D014466:Ultraviolet Rays; D014764:Viral Proteins / Q000032:analysis / Q000528:radiation effects*
chemical_list: D009698:Nucleoproteins; D012367:RNA, Viral; D012261:Ribonucleoproteins; D014764:Viral Proteins
vernacular_title: RNK-belkovye vzaimodeĭstviia v ribonukleoproteide virusa grippa A, vyiavliaemye pri UF-obluchenii.