Rational optimization of the DSL ligase ribozyme with GNRA/receptor interacting modules

Junya Ishikawa, Shigeyoshi Matsumura, Luc Jaeger, Tan Inoue, Hiroyuki Furuta, Yoshiya Ikawa

    Research output: Contribution to journalArticlepeer-review

    16 Citations (Scopus)


    The DSL ribozyme is a class of artificial ligase ribozymes with a highly modular architecture, which catalyzes template-directed RNA ligation on a helical substrate module that can be either covalently connected (cis-DSL) or physically separated (trans-DSL) from the catalytic module. Substrate recognition by the catalytic module is promoted by one or two sets of GNRA/receptor interactions acting as clamps in the cis or trans configurations, respectively. In this study, we have rationally designed and analyzed the catalytic and self-assembly properties of several trans-DSL ribozymes with different sets of natural and artificial GNRA-receptor clamps. Two variants newly designed in this study showed significantly enhanced catalytic properties with respect of the original trans-DSL construct. While this work allows dissection of the turnover and catalytic properties of the trans-DSL ribozyme, it also emphasizes the remarkable modularity of RNA tertiary structure for nano-construction of complex functions.

    Original languageEnglish
    Pages (from-to)163-170
    Number of pages8
    JournalArchives of Biochemistry and Biophysics
    Issue number2
    Publication statusPublished - Oct 15 2009

    All Science Journal Classification (ASJC) codes

    • Biophysics
    • Biochemistry
    • Molecular Biology


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