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dc.contributor.authorCorey, Robin
dc.contributor.authorAhdash, Zainab
dc.contributor.authorShah, Anokhi
dc.contributor.authorPyle, Euan
dc.contributor.authorAllen, William
dc.contributor.authorFessl, Thomas
dc.contributor.authorLovett, Janet Eleanor
dc.contributor.authorPolitis, Argyris
dc.contributor.authorCollinson, Ian
dc.date.accessioned2019-01-18T15:30:07Z
dc.date.available2019-01-18T15:30:07Z
dc.date.issued2019-01-02
dc.identifier.citationCorey , R , Ahdash , Z , Shah , A , Pyle , E , Allen , W , Fessl , T , Lovett , J E , Politis , A & Collinson , I 2019 , ' ATP-induced asymmetric pre-protein folding as a driver of protein translocation through the Sec machinery ' eLife , vol. 8 , e41803 . https://doi.org/10.7554/eLife.41803en
dc.identifier.issn2050-084X
dc.identifier.otherPURE: 257289746
dc.identifier.otherPURE UUID: 62c7bc60-db76-4755-a2ee-a068882c8853
dc.identifier.otherORCID: /0000-0002-3561-450X/work/52888777
dc.identifier.otherScopus: 85060026660
dc.identifier.otherWOS: 000455701200001
dc.identifier.urihttp://hdl.handle.net/10023/16900
dc.descriptionFunding: Royal Society for a University Research Fellowship; Wellcome Multi-User Equipment Grant (099149/Z/12/Z) (JEL).en
dc.description.abstractTransport of proteins across membranes is a fundamental process, achieved in every cell by the 'Sec' translocon. In prokaryotes, SecYEG associates with the motor ATPase SecA to carry out translocation for pre-protein secretion. Previously, we proposed a Brownian ratchet model for transport, whereby the free energy of ATP-turnover favours the directional diffusion of the polypeptide [Allen et al. eLife 2016]. Here, we show that ATP enhances this process by modulating secondary structure formation within the translocating protein. A combination of molecular simulation with hydrogen-deuterium-exchange mass spectrometry and electron paramagnetic resonance spectroscopy reveal an asymmetry across the membrane: ATP induced conformational changes in the cytosolic cavity promote unfolded pre-protein structure, while the exterior cavity favours its formation. This ability to exploit structure within a pre-protein is an unexplored area of protein transport, which may apply to other protein transporters, such as those of the endoplasmic reticulum and mitochondria.
dc.format.extent25
dc.language.isoeng
dc.relation.ispartofeLifeen
dc.rightsCopyright 2019 Corey et al. This article is distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use and redistribution provided that the original author and source are credited.en
dc.subjectQD Chemistryen
dc.subjectQH301 Biologyen
dc.subjectDASen
dc.subject.lccQDen
dc.subject.lccQH301en
dc.titleATP-induced asymmetric pre-protein folding as a driver of protein translocation through the Sec machineryen
dc.typeJournal articleen
dc.description.versionPublisher PDFen
dc.contributor.institutionUniversity of St Andrews.School of Physics and Astronomyen
dc.contributor.institutionUniversity of St Andrews.Biomedical Sciences Research Complexen
dc.identifier.doihttps://doi.org/10.7554/eLife.41803
dc.description.statusPeer revieweden


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