Design and analysis of a structural RNA that acts as a template for peptide ligation.

Norimasa Kashiwagi, Hiroyuki Furuta, Yoshiya Ikawa

    Research output: Contribution to journalArticlepeer-review

    3 Citations (Scopus)

    Abstract

    An artificial RNA, which acts as a specific template for peptide ligation, was designed and constructed. Into the P4-P6 domain of the Tetrahymena intron RNA, two peptide binding motifs (boxB and RRE) were installed. Two peptides (N and Rev) were expected to bind to the RNA simultaneously, facilitating their ligation by an entropic effect. The peptide ligation actually proceeded effectively in the presence of the designer RNA. Analysis using mutant peptides or mutant RNAs demonstrated that the peptide ligation proceeded by forming a specific trimolecular RNP complex.

    Original languageEnglish
    Pages (from-to)387-388
    Number of pages2
    JournalNucleic acids symposium series (2004)
    Issue number51
    DOIs
    Publication statusPublished - 2007

    All Science Journal Classification (ASJC) codes

    • General Medicine

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