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Journal of Biochemistry Advance Access published online on January 3, 2009
Journal of Biochemistry, doi:10.1093/jb/mvn183
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© The authors 2009. Published by Oxford University Press on behalf of the Japanese Biochemical Society. All rights reserved.

Concerted effects of two activator modules on the group I ribozyme reaction

Yoshiya Ikawa1,2, Tomoaki Shiohara3, Shoji Ohuchi4 and Tan Inoue3,5,*

1Department of Chemistry and Biochemistry, Graduate School of Engineering, Kyushu University, Fukuoka 819-0351, Japan
2PRESTO, Japan Science and Technology Agency, Japan
3Graduate School of Biostudies, Kyoto University, Kyoto 606-8502, Japan
4Department of Basic Medical Sciences, Institute of Medical Science, The University of Tokyo, Tokyo 108-8639, Japan
5ICORP, Japan Science and Technology Agency, Japan

*To whom correspondence should be addressed: Tan Inoue E-mail: tan{at}kuchem.kyoto-u.ac.jp.

Received November 17, 2008; Accepted November 28, 2008


  Abstract

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.


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