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

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 evo...

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Bibliographic Details
Published in:Nucleic acids research 2009-05, Vol.37 (8), p.2574-2583
Main Authors: Kashiwagi, Norimasa, Furuta, Hiroyuki, Ikawa, Yoshiya
Format: Article
Language:English
Subjects:
Amino Acid Sequence
Arginine - chemistry
Base Sequence
Binding Sites
Catalysis
Endonucleases - chemistry
Endonucleases - metabolism
Evolution, Molecular
Genetic Engineering
Molecular Sequence Data
Mutation
Nucleic Acid Conformation
Peptides - chemistry
Ribonucleoproteins - chemistry
RNA
RNA - chemistry
RNA, Catalytic - chemistry
RNA, Catalytic - metabolism
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Summary: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.
ISSN:0305-1048
1362-4962
DOI:10.1093/nar/gkp111