Journal
ELIFE
Volume 8, Issue -, Pages -Publisher
eLIFE SCIENCES PUBL LTD
DOI: 10.7554/eLife.41803
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Funding
- Biotechnology and Biological Sciences Research Council [BB/M003604/1, BB/1008675/1, BB/N015126/1]
- Wellcome [109854/Z/15/Z, 099149/Z/12/Z, 104632]
- Engineering and Physical Sciences Research Council [ep/m508214/1]
- European Regional Development Fund [CZ.02.1.01/0.0/0.0/15_003/0000441]
- Royal Society
- Wellcome Trust [099149/Z/12/Z, 109854/Z/15/Z] Funding Source: Wellcome Trust
- BBSRC [BB/M003604/1, BB/I008675/1, BB/N015126/1] Funding Source: UKRI
- EPSRC [EP/P020267/1, EP/L000253/1] Funding Source: UKRI
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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., 2016). Here, we show that ATP enhances this process by modulating secondary structure formation within the translocating protein. A combination of molecular simulation with hydrogendeuterium-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.
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