Journal
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA
Volume 107, Issue 26, Pages 11793-11798Publisher
NATL ACAD SCIENCES
DOI: 10.1073/pnas.1002356107
Keywords
chaperone; confinement; microfluidic mixing; FRET; fluorescence
Categories
Funding
- European Research Council
- Swiss National Center for Competence in Research for Structural Biology
- Swiss National Science Foundation
- VolkswagenStiftung
- Human Frontier Science Program
- Defense Microelectronics Activity (DMEA) Center for Nanoscience Innovation for Defense
- Forschungskredit of the University of Zurich
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Molecular chaperones are known to be essential for avoiding protein aggregation in vivo, but it is still unclear how they affect protein folding mechanisms. We use single-molecule Forster resonance energy transfer to follow the folding of a protein inside the GroEL/GroES chaperonin cavity over a time range from milliseconds to hours. Our results show that confinement in the chaperonin decelerates the folding of the C-terminal domain in the substrate protein rhodanese, but leaves the folding rate of the N-terminal domain unaffected. Microfluidic mixing experiments indicate that strong interactions of the substrate with the cavity walls impede the folding process, but the folding hierarchy is preserved. Our results imply that no universal chaperonin mechanism exists. Rather, a competition between intra-and intermolecular interactions determines the folding rates and mechanisms of a substrate inside the GroEL/GroES cage.
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