Folding and catalysis of the hairpin ribozyme

T. J. Wilson, M. Nahas, T. Ha, D. M.J. Lilley

Research output: Contribution to journalArticlepeer-review


The active form of the hairpin ribozyme is brought about by the interaction of two formally unpaired loops. In a natural molecule, these are present on two adjacent arms of a four-way junction. Although activity can be obtained in molecules lacking this junction, the junction is important in the promotion of the folded state of the ribozyme under physiological conditions, at a rate that is faster than the chemical reaction. Single-molecule fluorescence resonance energy transfer studies show that the junction introduces a discrete intermediate into the folding process, which repeatedly juxtaposes the two loops and thus promotes their docking. Using single-molecule enzymology, the cleavage and ligation rates have been measured directly. The pH dependence of the rates is consistent with a role for nucleobases acting in general acid-base catalysis.

Original languageEnglish (US)
Pages (from-to)461-465
Number of pages5
JournalBiochemical Society transactions
Issue number3
StatePublished - Jun 2005
Externally publishedYes


  • Acid-base catalysis
  • Fluorescence resonance energy transfer (FRET)
  • Hairpin ribozyme
  • RNA catalysis
  • Single-molecule spectroscopy

ASJC Scopus subject areas

  • Biochemistry


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