Folding and catalysis of the hairpin ribozyme

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

Research output: Contribution to journalArticle

Abstract

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
Volume33
Issue number3
DOIs
StatePublished - Jun 2005
Externally publishedYes

Fingerprint

Catalytic RNA
Fluorescence Resonance Energy Transfer
Catalysis
Ligation
Molecules
Acids
Chemical reactions
hairpin ribozyme

Keywords

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

ASJC Scopus subject areas

  • Biochemistry

Cite this

Folding and catalysis of the hairpin ribozyme. / Wilson, T. J.; Nahas, M.; Ha, Taekjip; Lilley, D. M J.

In: Biochemical Society Transactions, Vol. 33, No. 3, 06.2005, p. 461-465.

Research output: Contribution to journalArticle

Wilson, T. J. ; Nahas, M. ; Ha, Taekjip ; Lilley, D. M J. / Folding and catalysis of the hairpin ribozyme. In: Biochemical Society Transactions. 2005 ; Vol. 33, No. 3. pp. 461-465.
@article{63d066ce4fc94ab1960d176d43f8c3fe,
title = "Folding and catalysis of the hairpin ribozyme",
abstract = "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.",
keywords = "Acid-base catalysis, Fluorescence resonance energy transfer (FRET), Hairpin ribozyme, RNA catalysis, Single-molecule spectroscopy",
author = "Wilson, {T. J.} and M. Nahas and Taekjip Ha and Lilley, {D. M J}",
year = "2005",
month = "6",
doi = "10.1042/BST0330461",
language = "English (US)",
volume = "33",
pages = "461--465",
journal = "Biochemical Society Transactions",
issn = "0300-5127",
publisher = "Portland Press Ltd.",
number = "3",

}

TY - JOUR

T1 - Folding and catalysis of the hairpin ribozyme

AU - Wilson, T. J.

AU - Nahas, M.

AU - Ha, Taekjip

AU - Lilley, D. M J

PY - 2005/6

Y1 - 2005/6

N2 - 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.

AB - 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.

KW - Acid-base catalysis

KW - Fluorescence resonance energy transfer (FRET)

KW - Hairpin ribozyme

KW - RNA catalysis

KW - Single-molecule spectroscopy

UR - http://www.scopus.com/inward/record.url?scp=21044455455&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=21044455455&partnerID=8YFLogxK

U2 - 10.1042/BST0330461

DO - 10.1042/BST0330461

M3 - Article

C2 - 15916541

AN - SCOPUS:21044455455

VL - 33

SP - 461

EP - 465

JO - Biochemical Society Transactions

JF - Biochemical Society Transactions

SN - 0300-5127

IS - 3

ER -