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

Norimasa Kashiwagi, Hiroyuki Furuta, Yoshiya Ikawa

Research output: Contribution to journalArticle

11 Citations (Scopus)

Abstract

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.

Original languageEnglish
Pages (from-to)2574-2583
Number of pages10
JournalNucleic acids research
Volume37
Issue number8
DOIs
Publication statusPublished - 2009

All Science Journal Classification (ASJC) codes

  • Genetics

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