期刊
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA
卷 105, 期 37, 页码 13853-13858出版社
NATL ACAD SCIENCES
DOI: 10.1073/pnas.0804034105
关键词
multidomain RNA folding; single-molecule Forster resonance energy transfer; splicing; structural dynamics; metal ions
资金
- University of Zurich
- Swiss National Science Foundation SNF-Forderungsprofessur
- Wayne State University
- National Institutes of Health [GM GM085116]
- National Science Foundation CAREER [0747285]
- Direct For Biological Sciences
- Div Of Molecular and Cellular Bioscience [0747285] Funding Source: National Science Foundation
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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