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Forces on Nascent Polypeptides during Membrane Insertion and Translocation via the Sec Translocon
Stockholm University, Faculty of Science, Department of Biochemistry and Biophysics.
Stockholm University, Faculty of Science, Department of Biochemistry and Biophysics.
Stockholm University, Faculty of Science, Department of Biochemistry and Biophysics.
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Number of Authors: 52018 (English)In: Biophysical Journal, ISSN 0006-3495, E-ISSN 1542-0086, Vol. 115, no 10, p. 1885-1894Article in journal (Refereed) Published
Abstract [en]

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.

Place, publisher, year, edition, pages
2018. Vol. 115, no 10, p. 1885-1894
National Category
Biological Sciences
Identifiers
URN: urn:nbn:se:su:diva-162771DOI: 10.1016/j.bpj.2018.10.002ISI: 000450765100006PubMedID: 30366631OAI: oai:DiVA.org:su-162771DiVA, id: diva2:1274230
Available from: 2018-12-28 Created: 2018-12-28 Last updated: 2018-12-28Bibliographically approved

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