Functional domain-assembly in hairpin ribozymes.
Functional structures of hairpin ribozymes have been investigated by constructing various chemically modified molecules. Domain-exchange and linker insertion experiments were performed to find active conformations of the RNA enzyme showing cleavage activity. Our experiments and other evidence suggest that the active structure has a bent conformation, and that domain-interactions are essential for the cleavage activity.
Komatsu
Y
Y
Graduate School of Pharmaceutical Sciences, Hokkaido University, Sapporo 060-0812, Japan. ohtsuka@pharm.hokudai.ac.jp
Kanzaki
I
I
Shirai
M
M
Kumagai
I
I
Yamashita
S
S
Ohtsuka
E
E
D017860:Nepovirus / Q000235:genetics; D009690:Nucleic Acid Conformation; D012313:RNA / Q000737:chemistry / Q000378:metabolism; D016337:RNA, Catalytic / Q000737:chemistry* / Q000378:metabolism; D012367:RNA, Viral / Q000737:chemistry* / Q000378:metabolism; D013379:Substrate Specificity; D014158:Transcription, Genetic
D016337:RNA, Catalytic; D012367:RNA, Viral; C039919:RNA, recombinant; D012313:RNA