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Nucleic Acids Research Advance Access originally published online on March 5, 2009
Nucleic Acids Research 2009 37(8):2574-2583; doi:10.1093/nar/gkp111
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Nucleic Acids Research, 2009, Vol. 37, No. 8 2574-2583
© 2009 The Author(s)
This is an Open Access article distributed under the terms of the Creative Commons Attribution Non-Commercial License (http://creativecommons.org/licenses/by-nc/2.0/uk/) which permits unrestricted non-commercial use, distribution, and reproduction in any medium, provided the original work is properly cited.

RNA

Primitive templated catalysis of a peptide ligation by self-folding RNAs

Norimasa Kashiwagi1, Hiroyuki Furuta1 and Yoshiya Ikawa1,2,*

1Department of Chemistry and Biochemistry, Graduate School of Engineering, Kyushu University, 744 Moto-oka, Nishi-ku, Fukuoka 819-0395 and 2PRESTO, Precursory Research for Embryonic Science and Technology, Japan Science and Technology Agency, Tokyo 102-0075, Japan

*To whom correspondence should be addressed. Tel: +81 92 802 2866; Fax: +81 92 802 2865; Email: yikawa{at}cstf.kyushu-u.ac.jp

Received August 21, 2008. Revised February 3, 2009. Accepted February 3, 2009.

RNA–polypeptide complexes (RNPs), which play various roles in extant biological systems, have been suggested to have been important in the early stages of the molecular evolution of life. At a certain developmental stage of ancient RNPs, their RNA and polypeptide components have been proposed to evolve in a reciprocal manner to establish highly elaborate structures and functions. We have constructed a simple model system, from which a cooperative evolution system of RNA and polypeptide components could be developed. Based on the observation that several RNAs modestly accelerated the chemical ligation of the two basic peptides. We have designed an RNA molecule possessing two peptide binding sites that capture the two peptides. This designed RNA can also accelerate the peptide ligation. The resulting ligated peptide, which has two RNA-binding sites, can in turn function as a trans-acting factor that enhances the endonuclease activity catalyzed by the designed RNA.


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