Folding and catalysis by the VS ribozyme

Daniel A. Lafontaine; David G. Norman; David M.J. Lilley

doi:10.1016/S0300-9084(02)01406-2

Folding and catalysis by the VS ribozyme

Daniel A. Lafontaine, David G. Norman, David M.J. Lilley (Lead / Corresponding author)

Research output: Contribution to journal › Article › peer-review

9 Citations (Scopus)

Abstract

The VS ribozyme is a 154 nt self-cleaving RNA molecule that can be divided into a trans-acting five-helix ribozyme and stem-loop substrate. The structure of the ribozyme is organised by two three-way helical junctions, the structure of which has been determined by a combination of comparative gel electrophoresis and fluorescence resonance energy transfer experiments. From this, the overall global architecture of the ribozyme has been deduced. The substrate is then thought to dock into the cleft formed between helices II and VI, where it makes a close interaction with the loop containing A730. The A730 loop is the probable active site of the ribozyme, and A756 within it is a strong candidate to play a direct role in the transesterification chemistry, possibly by general acid-base catalysis.

Original language	English
Pages (from-to)	889-896
Number of pages	8
Journal	Biochimie
Volume	84
Issue number	9
DOIs	https://doi.org/10.1016/S0300-9084(02)01406-2
Publication status	Published - 1 Sept 2002

Keywords

Metal ions
RNA catalysis
RNA folding
RNA structure

ASJC Scopus subject areas

Biochemistry

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10.1016/S0300-9084(02)01406-2

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title = "Folding and catalysis by the VS ribozyme",

abstract = "The VS ribozyme is a 154 nt self-cleaving RNA molecule that can be divided into a trans-acting five-helix ribozyme and stem-loop substrate. The structure of the ribozyme is organised by two three-way helical junctions, the structure of which has been determined by a combination of comparative gel electrophoresis and fluorescence resonance energy transfer experiments. From this, the overall global architecture of the ribozyme has been deduced. The substrate is then thought to dock into the cleft formed between helices II and VI, where it makes a close interaction with the loop containing A730. The A730 loop is the probable active site of the ribozyme, and A756 within it is a strong candidate to play a direct role in the transesterification chemistry, possibly by general acid-base catalysis.",

keywords = "Metal ions, RNA catalysis, RNA folding, RNA structure",

author = "Lafontaine, {Daniel A.} and Norman, {David G.} and Lilley, {David M.J.}",

note = "Funding Information: We thank our colleagues Tim Wilson and Christian Hammann for discussion, and Cancer Research UK and the BBSRC for financial support.",

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T1 - Folding and catalysis by the VS ribozyme

AU - Lafontaine, Daniel A.

AU - Norman, David G.

AU - Lilley, David M.J.

N1 - Funding Information: We thank our colleagues Tim Wilson and Christian Hammann for discussion, and Cancer Research UK and the BBSRC for financial support.

PY - 2002/9/1

Y1 - 2002/9/1

N2 - The VS ribozyme is a 154 nt self-cleaving RNA molecule that can be divided into a trans-acting five-helix ribozyme and stem-loop substrate. The structure of the ribozyme is organised by two three-way helical junctions, the structure of which has been determined by a combination of comparative gel electrophoresis and fluorescence resonance energy transfer experiments. From this, the overall global architecture of the ribozyme has been deduced. The substrate is then thought to dock into the cleft formed between helices II and VI, where it makes a close interaction with the loop containing A730. The A730 loop is the probable active site of the ribozyme, and A756 within it is a strong candidate to play a direct role in the transesterification chemistry, possibly by general acid-base catalysis.

AB - The VS ribozyme is a 154 nt self-cleaving RNA molecule that can be divided into a trans-acting five-helix ribozyme and stem-loop substrate. The structure of the ribozyme is organised by two three-way helical junctions, the structure of which has been determined by a combination of comparative gel electrophoresis and fluorescence resonance energy transfer experiments. From this, the overall global architecture of the ribozyme has been deduced. The substrate is then thought to dock into the cleft formed between helices II and VI, where it makes a close interaction with the loop containing A730. The A730 loop is the probable active site of the ribozyme, and A756 within it is a strong candidate to play a direct role in the transesterification chemistry, possibly by general acid-base catalysis.

KW - Metal ions

KW - RNA catalysis

KW - RNA folding

KW - RNA structure

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U2 - 10.1016/S0300-9084(02)01406-2

DO - 10.1016/S0300-9084(02)01406-2

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AN - SCOPUS:0036761233

SN - 0300-9084

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EP - 896

JO - Biochimie

JF - Biochimie

IS - 9

ER -

Folding and catalysis by the VS ribozyme

Abstract

Keywords

ASJC Scopus subject areas

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