title: TectoRNP: self-assembling RNAs with peptide recognition motifs as templates for chemical peptide ligation.
abstract: TectoRNA, an artificial RNA with self-assembling ability, has been employed as a structural platform for RNA nanotechnology and RNA synthetic biology. In this study, tectoRNA was applied as a specific template for chemical peptide ligation. On the basis of a self-assembling tectoRNA, we designed and constructed a template RNA that facilitates peptide ligation depending on controlled dimer formation. Two RNA-binding peptides were recognized by two peptide-binding RNA motifs embedded in the template RNA, and chemical ligation was promoted because of the entropic effect of Mg(2+) -dependent dimerization. In a series of biochemical analyses, we determined the relationship between the structures of the tectoRNA-based templates and the extent of acceleration in peptide ligation.
authors.affiliation: Department of Chemistry and Biochemistry, Graduate School of Engineering, Kyushu University, Moto-oka 744, Nishi-ku, Fukuoka, 819-0395, Japan.
authors.forename: Kohei
authors.initials: K
authors.lastname: Yamashita
authors.forename: Takahiro
authors.initials: T
authors.lastname: Tanaka
authors.forename: Hiroyuki
authors.initials: H
authors.lastname: Furuta
authors.forename: Yoshiya
authors.initials: Y
authors.lastname: Ikawa
mesh_terms: D020816:Amino Acid Motifs; D019281:Dimerization; D008274:Magnesium / Q000737:chemistry; D010455:Peptides / Q000138:chemical synthesis* / Q000737:chemistry*; D012313:RNA / Q000737:chemistry*; D012261:Ribonucleoproteins / Q000138:chemical synthesis* / Q000737:chemistry*
chemical_list: D010455:Peptides; D012261:Ribonucleoproteins; D012313:RNA; D008274:Magnesium