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ATP-induced asymmetric pre-protein folding as a driver of protein translocation through the Sec machinery
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dc.contributor.author | Corey, Robin | |
dc.contributor.author | Ahdash, Zainab | |
dc.contributor.author | Shah, Anokhi | |
dc.contributor.author | Pyle, Euan | |
dc.contributor.author | Allen, William | |
dc.contributor.author | Fessl, Thomas | |
dc.contributor.author | Lovett, Janet Eleanor | |
dc.contributor.author | Politis, Argyris | |
dc.contributor.author | Collinson, Ian | |
dc.date.accessioned | 2019-01-18T15:30:07Z | |
dc.date.available | 2019-01-18T15:30:07Z | |
dc.date.issued | 2019-01-02 | |
dc.identifier | 257289746 | |
dc.identifier | 62c7bc60-db76-4755-a2ee-a068882c8853 | |
dc.identifier | 000455701200001 | |
dc.identifier | 85060026660 | |
dc.identifier.citation | Corey , 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.41803 | en |
dc.identifier.issn | 2050-084X | |
dc.identifier.other | ORCID: /0000-0002-3561-450X/work/52888777 | |
dc.identifier.uri | https://hdl.handle.net/10023/16900 | |
dc.description | Funding: Royal Society for a University Research Fellowship; Wellcome Multi-User Equipment Grant (099149/Z/12/Z) (JEL). | en |
dc.description.abstract | Transport 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.extent | 25 | |
dc.format.extent | 5448889 | |
dc.language.iso | eng | |
dc.relation.ispartof | eLife | en |
dc.subject | QD Chemistry | en |
dc.subject | QH301 Biology | en |
dc.subject | DAS | en |
dc.subject.lcc | QD | en |
dc.subject.lcc | QH301 | en |
dc.title | ATP-induced asymmetric pre-protein folding as a driver of protein translocation through the Sec machinery | en |
dc.type | Journal article | en |
dc.contributor.sponsor | The Royal Society | en |
dc.contributor.sponsor | The Wellcome Trust | en |
dc.contributor.institution | University of St Andrews. School of Physics and Astronomy | en |
dc.contributor.institution | University of St Andrews. Biomedical Sciences Research Complex | en |
dc.identifier.doi | 10.7554/eLife.41803 | |
dc.description.status | Peer reviewed | en |
dc.identifier.grantnumber | UF150698 | en |
dc.identifier.grantnumber | 099149/Z/12/Z | en |
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