- Mathieu Botte
- Nathan Zaccai
- Jelger Lycklama a Nijeholt
- Remy Martin
- Kevin Knoops
- Gabor Papai
- Juan Zou
- Aurelien Deniaud
- Manikandan Karuppasamy
- Qiyang Jiang
- Abhishek Singha Roy
- Klaus Schulten
- Patrick Schultz
- Juri Rappsilber
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Final published version, 1 MB, PDF document
Licence: Creative Commons: Attribution (CC-BY)
Original language | English |
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Article number | 38399 |
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Journal | Scientific Reports |
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Early online date | 7 Dec 2016 |
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DOIs | |
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Publication status | E-pub ahead of print - 7 Dec 2016 |
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The conserved SecYEG protein-conducting channel and the accessory proteins SecDF-YajC and YidC constitute the bacterial holo-translocon (HTL), capable of protein-secretion and membrane-protein insertion. By employing an integrative approach combining small-angle neutron scattering (SANS), low-resolution electron microscopy and biophysical analyses we determined the arrangement of the proteins and lipids within the supercomplex. The results guided the placement of X-ray structures of individual HTL components and allowed the proposal of a model of the functional translocon. Their arrangement around a central lipid-containing pool conveys an unexpected, but compelling mechanism for membrane-protein insertion. The periplasmic domains of YidC and SecD are poised at the protein-channel exit-site of SecY, presumably to aid the emergence of translocating polypeptides. The SecY lateral gate for membrane-insertion is adjacent to the membrane ‘insertase’ YidC. Absolute-scale SANS employing a novel contrast-match-point analysis revealed a dynamic complex adopting open and compact configurations around an adaptable central lipid-filled chamber, wherein polytopic membrane-proteins could fold, sheltered from aggregation and proteolysis.
ID: 29599714