title: [Comparison of the conformation of RNA from phage MS2 and 16S rRNA. Accessibility to nucleases S1 and SV specific to secondary structure and thermal stability].
abstract: The hydrolysis of E. coli 16S rRNA by nucleases specific to the secondary structure elements (S1 and SV), the melting of the RNA after partial hydrolysis by nuclease S1 and the electrophoretic mobility of hydrolysis products after denaturation-renaturation of RNA were studied. It was shown that the sensitivity of 16S rRNA to nuclease S1 depends on Zn or Mg ions concentration. The melting curves after partial hydrolysis by nuclease S1 were characterized by a decrease of the hyperchromic effect (by approximately 15%) and by a increase of Tm (by 3 degrees). After RNA denaturation followed by slow or fast renaturation the electrophoretic patterns of the hydrolysis products were not changed, as in the case of phage MS2 RNA. It was supposed, that the rRNA molecule has a stable "nucleus" (or "nuclei"), which is organized as an intramolecular association of parallelly oriented double-stranded fragments of this RNA. Previously, such a mode of the spatial organization was proposed by us for phage MS2 RNA.
mesh_terms: D003090:Coliphages / Q000235:genetics; D004720:Endonucleases; D004722:Endoribonucleases; D004926:Escherichia coli / Q000235:genetics; D006358:Hot Temperature; D006868:Hydrolysis; D007700:Kinetics; D009690:Nucleic Acid Conformation; D009691:Nucleic Acid Denaturation; D012329:RNA, Bacterial; D012335:RNA, Ribosomal; D012367:RNA, Viral; D015719:Single-Strand Specific DNA and RNA Endonucleases
chemical_list: D012329:RNA, Bacterial; D012335:RNA, Ribosomal; D012367:RNA, Viral; D004720:Endonucleases; D004722:Endoribonucleases; C043004:cobra venom endonuclease; D015719:Single-Strand Specific DNA and RNA Endonucleases
vernacular_title: Sravnenie prostranstvennoĭ organizatsii RNK faga MS2 i 16S rRNK. Dostupnost' nukleazam S1 i SV, spetsifichnym ko vtorichnoĭ strukture, i termicheskaia ustoĭchivost'.