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 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.
Kashiwagi
Norimasa
N
Department of Chemistry and Biochemistry, Graduate School of Engineering, Kyushu University, 744 Moto-oka, Nishi-ku, Fukuoka 819-0395, Japan.
Furuta
Hiroyuki
H
Ikawa
Yoshiya
Y
D000595:Amino Acid Sequence; D001120:Arginine / Q000737:chemistry; D001483:Base Sequence; D001665:Binding Sites; D002384:Catalysis; D004720:Endonucleases / Q000737:chemistry / Q000378:metabolism; D019143:Evolution, Molecular; D005818:Genetic Engineering; D008969:Molecular Sequence Data; D009154:Mutation; D009690:Nucleic Acid Conformation; D010455:Peptides / Q000737:chemistry*; D012313:RNA / Q000737:chemistry*; D016337:RNA, Catalytic / Q000737:chemistry / Q000378:metabolism; D012261:Ribonucleoproteins / Q000737:chemistry
D010455:Peptides; D016337:RNA, Catalytic; D012261:Ribonucleoproteins; D012313:RNA; D001120:Arginine; D004720:Endonucleases