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Conversation 11: No. 1

category image Volume: Conversation 11
Issue Number 1
May 2000
ISBN 0-940030-80-2

RNA Scaffolds for Minihelix-Based Aminoacyl Transfer: Design of ?Transpeptizymes?

Some evidence and considerations suggest that RNA minihelices based on the acceptor-TYC stem-loop of tRNAs are the historical, more ancient part of the tRNA structure. These minihelices are substrates for aminoacylation by tRNA synthetases. In the transition from the RNA world to the theatre of proteins, aminoacyl minihelices may have had a role in early systems of peptide synthesis. Such systems would require bringing together aminoacyl groups into close proximity in order for peptide bonds to form. Here we report the design of RNA scaffolds based on pieces of the structure of the P4-P6 domain of the Tetrahymena ribozyme. RNA minihelices were incorporated into these scaffolds and the resulting RNAs could be enzymatically aminoacylated. The RNA scaffolds containing the minihelix-like pieces associated spontaneously to create the presumptive P4-P6 structure and thereby bring together the substrates for aminoacylation. Thus, peptide synthesis with associating RNA scaffolds that contain minihelix-like motifs appears plausible.

Niranjan Y. Sardesai1
Scott M. Stagg2
Margaret S. VanLoock2
Stephen C. Harvey2
and Paul Schimmel1

1 The Skaggs Institute for Chemical Biology
The Scripps Research Institute
10550 North Torrey Pines Road
La Jolla, CA 92037
2 Department of Biochemistry and Molecular Genetics
University of Alabama at Birmingham
Birmingham, AL 35294

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