Journal Article

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

Norimasa Kashiwagi, Hiroyuki Furuta and Yoshiya Ikawa

in Nucleic Acids Research

Volume 37, issue 8, pages 2574-2583
Published in print May 2009 | ISSN: 0305-1048
Published online March 2009 | e-ISSN: 1362-4962 | DOI: http://dx.doi.org/10.1093/nar/gkp111

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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.

Journal Article.  5086 words.  Illustrated.

Subjects: Chemistry ; Biochemistry ; Bioinformatics and Computational Biology ; Genetics and Genomics ; Molecular and Cell Biology

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