Evidence that genomic and antigenomic RNA self-cleaving elements from hepatitis delta virus have similar secondary structures.
The two sequences that define the self-cleaving elements from the genomic and antigenomic RNA of hepatitis delta virus were folded into secondary structures with similar features. Evidence in support of the two models was obtained from limited ribonuclease digestion of genomic and antigenomic RNA fragments containing the sequence 3' of the cleavage site. Under conditions where the rates of self-cleavage are enhanced by addition of 5 M urea (2-10 mM Mg2+ at 37 degrees C), ribonucleases T1, U2, A and V1 generated digestion patterns consistent with the proposed RNA structures. The evidence for a relatively stable structure in urea when Mg2+ is present suggests that denaturant-enhanced rates of self-cleavage could result from destabilization of competing inactive structures.
Department of Biochemistry, Duke University Medical Center, Durham, NC 27710.
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Rosenstein
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Been
D004591:Electrophoresis, Polyacrylamide Gel; D004722:Endoribonucleases / Q000378:metabolism; D003698:Hepatitis Delta Virus / Q000235:genetics*; D007700:Kinetics; D008274:Magnesium / Q000378:metabolism; D008958:Models, Molecular; D009690:Nucleic Acid Conformation; D016337:RNA, Catalytic / Q000737:chemistry* / Q000378:metabolism; D012367:RNA, Viral / Q000737:chemistry* / Q000378:metabolism; D006163:Ribonuclease T1 / Q000378:metabolism; D012259:Ribonuclease, Pancreatic / Q000378:metabolism; D014508:Urea / Q000378:metabolism
D016337:RNA, Catalytic; D012367:RNA, Viral; D014508:Urea; D004722:Endoribonucleases; C032825:ribonuclease V(1); D006163:Ribonuclease T1; C022544:ribonuclease U2; D012259:Ribonuclease, Pancreatic; D008274:Magnesium