Journal
BIOPHYSICAL JOURNAL
Volume 115, Issue 10, Pages 1885-1894Publisher
CELL PRESS
DOI: 10.1016/j.bpj.2018.10.002
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Funding
- Knut and Alice Wallenberg Foundation
- Swedish Cancer Foundation
- Swedish Research Council
- National Institutes of Health [R01GM125063]
- Office of Naval Research [N00014-16-1-2761]
- Office of Science of the US Department of Energy [DE-AC02-05CH11231]
- Extreme Science and Engineering Discovery Environment [40]
- National Science Foundation [ACI-1548562]
- NATIONAL INSTITUTE OF GENERAL MEDICAL SCIENCES [R01GM125063] Funding Source: NIH RePORTER
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During ribosomal translation, nascent polypeptide chains (NCs) undergo a variety of physical processes that determine their fate in the cell. This study utilizes a combination of arrest peptide experiments and coarse-grained molecular dynamics to measure and elucidate the molecular origins of forces that are exerted on NCs during cotranslational membrane insertion and translocation via the Sec translocon. The approach enables deconvolution of force contributions from NC-translocon and NC-ribosome interactions, membrane partitioning, and electrostatic coupling to the membrane potential. In particular, we show that forces due to NC-lipid interactions provide a readout of conformational changes in the Sec translocon, demonstrating that lateral gate opening only occurs when a sufficiently hydrophobic segment of NC residues reaches the translocon. The combination of experiment and theory introduced here provides a detailed picture of the molecular interactions and conformational changes during ribosomal translation that govern protein biogenesis.
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