The accessibility of phage MS2 RNA to structure specific nucleases in various conditions.
The accessibility of ds- and ss-segments of phage MS2 RNA to ds- and ss-specific nucleases (RNase III, nuclease SV and nuclease S1) was studied. The results show that the RNA has hydrolysis sites for all the nucleases used. These sites are unvariable in a wide range of the conditions (ionic strength, pH, bivalent cations and temperature) and are not changed also after denaturation-renaturation of the RNA. This testifies that the distribution and interactions of ds- and ss-segments in the whole molecule are very specific and stable.
Grechko
V V
VV
Tymokhina
G I
GI
Aleshkina
L A
LA
Kalashnikova
J I
JI
Majev
S P
SP
Vassilenko
S K
SK
D001435:Bacteriophages / Q000378:metabolism*; D001665:Binding Sites; D004720:Endonucleases / Q000378:metabolism; D004722:Endoribonucleases / Q000378:metabolism; D006868:Hydrolysis; D012330:RNA, Double-Stranded / Q000378:metabolism; D012367:RNA, Viral / Q000378:metabolism*; D043244:Ribonuclease III; D012260:Ribonucleases / Q000378:metabolism*; D015719:Single-Strand Specific DNA and RNA Endonucleases
D012330:RNA, Double-Stranded; D012367:RNA, Viral; D004720:Endonucleases; D004722:Endoribonucleases; D012260:Ribonucleases; C043004:cobra venom endonuclease; D043244:Ribonuclease III; D015719:Single-Strand Specific DNA and RNA Endonucleases