Concerted effects of two activator modules on the group I ribozyme reaction.
Group I intron ribozymes have a modular architecture and structural elements essential for catalysis. The elements are located in the conserved modular domain P3-P7 that is stabilized by another conserved module, P4-P6. It has been reported that artificial modules can complement the function of the native P4-P6. To exploit the modular architecture of group I ribozyme, we have constructed a hybrid ribozyme by attaching an artificial activator module to the wild-type T4 td ribozyme. Kinetic analysis of the hybrid ribozyme revealed that the artificial module and P4-P6 have unusual positive and negative concerted effects in activating the ribozyme.
Ikawa
Yoshiya
Y
Department of Chemistry and Biochemistry, Graduate School of Engineering, Kyushu University, Fukuoka 819-0351, Japan.
Shiohara
Tomoaki
T
Ohuchi
Shoji
S
Inoue
Tan
T
D017122:Bacteriophage T4 / Q000201:enzymology; D001483:Base Sequence; D004789:Enzyme Activation / Q000187:drug effects; D019143:Evolution, Molecular; D007438:Introns / Q000235:genetics; D007700:Kinetics; D008274:Magnesium / Q000494:pharmacology; D008958:Models, Molecular; D008969:Molecular Sequence Data; D009690:Nucleic Acid Conformation; D016337:RNA, Catalytic / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism*; D013379:Substrate Specificity / Q000187:drug effects
C116167:GIR1 ribozyme; D016337:RNA, Catalytic; D008274:Magnesium