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Single molecule studies of group II intron ribozymes


Steiner, M; Karunatilaka, K S; Sigel, R K O; Rueda, D (2008). Single molecule studies of group II intron ribozymes. Proceedings of the National Academy of Sciences of the United States of America (PNAS), 105(37):13853-13858.

Abstract

Group II intron ribozymes fold into their native structure by a unique stepwise process that involves an initial slow compaction followed by fast formation of the native state in a Mg2+-dependent manner.
Single-molecule fluorescence reveals three distinct on-pathway conformations in dynamic equilibrium connected by relatively small activation barriers. From a most stable near-native state, the unobserved catalytically active conformer is reached. This most compact conformer occurs only transiently above 20 mM Mg2+ and is stabilized by substrate binding, which together explain the slow cleavage of the ribozyme. Structural dynamics increase with increasing Mg2+ concentrations, enabling the enzyme to reach its active state.

Group II intron ribozymes fold into their native structure by a unique stepwise process that involves an initial slow compaction followed by fast formation of the native state in a Mg2+-dependent manner.
Single-molecule fluorescence reveals three distinct on-pathway conformations in dynamic equilibrium connected by relatively small activation barriers. From a most stable near-native state, the unobserved catalytically active conformer is reached. This most compact conformer occurs only transiently above 20 mM Mg2+ and is stabilized by substrate binding, which together explain the slow cleavage of the ribozyme. Structural dynamics increase with increasing Mg2+ concentrations, enabling the enzyme to reach its active state.

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Additional indexing

Item Type:Journal Article, refereed, original work
Communities & Collections:07 Faculty of Science > Department of Chemistry
Dewey Decimal Classification:540 Chemistry
Uncontrolled Keywords:multidomain RNA folding, single-molecule Förster resonance energy transfer, splicing, structural dynamics, metal ions
Language:English
Date:16 September 2008
Deposited On:02 Dec 2008 15:54
Last Modified:05 Apr 2016 12:35
Publisher:National Academy of Sciences
ISSN:0027-8424
Additional Information:Copyright: National Academy of Sciences USA
Publisher DOI:10.1073/pnas.0804034105
Official URL:http://www.pnas.org/content/early/2008/09/03/0804034105
PubMed ID:18772388
Permanent URL: http://doi.org/10.5167/uzh-5890

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