Open AccessAn RNA Binding Peptide Consisting of Four Types of Amino Acid by in Vitro Selection Using cDNA Display
Author(s) -
Shigefumi Kumachi,
Yuzuru Husimi,
Naoto Nemoto
Publication year - 2016
Publication title -
acs omega
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.779
H-Index - 40
ISSN - 2470-1343
DOI - 10.1021/acsomega.6b00015
Subject(s) - rna , complementary dna , peptide , in vitro , amino acid , biology , cdna library , peptide sequence , biochemistry , transfer rna , microbiology and biotechnology , computational biology , chemistry , gene
RNA-protein interactions have a central role in the living world. In this article, we examined whether primitive peptides (30 residues) consisting of four types of amino acid (Gly, Ala, Asp, and Val) could interact with tRNA as a model of primitive RNAs in the RNA world. By in vitro selection of binding peptides using the cDNA display method, a characteristic peptide was selected from a random peptide library and assayed by electrophoretic mobility shift and pull-down assays. Interestingly, the selected peptide bound to a single-stranded region including a loop structure of an RNA molecule with some sequence specificity.