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Nucleic Acids Symposium Series 2009 53(1):35-36; doi:10.1093/nass/nrp018
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© 2009 Oxford University Press

This article appears in the following Nucleic Acid Symposium Series issue: The 6th International Symposium on Nucleic Acids Chemistry (36th Symposium on Nucleic Acids Chemistry) [View the issue table of contents]

Substrate recognition of pre-tRNA by ribonuclease P --- subsite model of natural ribozyme originated from Escherichia coli

Akihiro Fujimoto, Yo Kikuchi and Terumichi Tanaka

Division of Bioscience and Biotechnology, Department of Ecological Engineering, Toyohashi University of Technology, 1-1 Hibarigaoka, Tempaku-cho, Toyohashi, Aichi 441-8580, Japan

*Corresponding author. E-mail: tanakat{at}eco.tut.ac.jp

Abstract

Combination of cleavage site analysis and kinetic analysis of a series of shape variant of pre-tRNA substrate, we newly found two subsites which contribute to recognition of shape in substrate binding and catalysis by bacterial RNase P. Our data showed that the ribozyme traps the substrate by 5'- and 3'-end regions to form Michaelis complex, and after that the shape of the substrat is examied by other two subsites in the transition state. In the meeting, we will show the posibility that the S-domain can contribute to stabilize the transition state of the cleavage reaction of a pre-tRNA substrate.


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