Coordinated control of a designed trans-acting ligase ribozyme by a loop-receptor interaction

FEBS Lett. 2009 Sep 3;583(17):2819-26. doi: 10.1016/j.febslet.2009.07.036. Epub 2009 Jul 23.

Abstract

We previously developed a synthetic cis-acting RNA ligase ribozyme with 3'-5' joining activity termed "DSL" (designed and selected ligase). DSL was easily transformed into a trans-acting form because of its highly modular architecture. In this study, we investigated the modular properties and turnover capabilities of a trans-acting DSL, tDSL-1/GUAA. tDSL-1/GUAA exhibited remarkably high activity compared with the parental cis-acting DSL, and it attained a high turnover number. Taken together, the results indicate that a loop-receptor interaction plays a significant role in determining the activity of the trans-acting ribozyme and in its ability to perform multiple turnovers of the reaction.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Base Pairing
  • Base Sequence
  • Molecular Sequence Data
  • Nucleic Acid Conformation*
  • RNA Ligase (ATP) / chemistry*
  • RNA Ligase (ATP) / genetics
  • RNA Ligase (ATP) / metabolism*
  • RNA, Catalytic / chemistry*
  • RNA, Catalytic / genetics
  • RNA, Catalytic / metabolism*
  • Substrate Specificity

Substances

  • RNA, Catalytic
  • RNA Ligase (ATP)