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The ribosome modulates nascent protein folding
Christian M Kaiser1, Daniel H Goldman, John D Chodera
1Institute for Quantitative Biosciences , University of California-Berkeley, CA 94720, USA.
Science (New York, N.Y.)
|December 24, 2011
Summary
The ribosome influences protein folding. It slows native state attainment but prevents misfolding and aggregation for nascent polypeptides, promoting efficient de novo folding.
Area of Science:
- Molecular Biology
- Biophysics
Background:
- Proteins require proper folding to become active after synthesis by ribosomes.
- The ribosome's role in protein folding has been hypothesized but difficult to prove experimentally.
Purpose of the Study:
- To investigate the influence of the ribosome on the folding of nascent polypeptides.
- To determine if the ribosome affects the kinetics and fidelity of protein folding.
Main Methods:
- Development of an experimental system using optical tweezers.
- Studying single ribosome-bound stalled nascent polypeptides during in vitro translation.
- Utilizing T4 lysozyme as a model protein.
Main Results:
- The ribosome slows the formation of stable tertiary interactions and native state attainment for T4 lysozyme compared to free protein.
- Incomplete polypeptides prone to misfolding and aggregation in solution remain folding-competent near the ribosome.
- The ribosome's surface environment appears to support folding competence.
Conclusions:
- The ribosome plays a crucial role beyond synthesis, actively promoting efficient de novo protein folding.
- Ribosome-bound nascent chains exhibit distinct folding behavior compared to free polypeptides.
- The ribosome facilitates the attainment of the native state and prevents misfolding near its surface.
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