Journal
SCIENTIFIC REPORTS
Volume 6, Issue -, Pages -Publisher
NATURE PUBLISHING GROUP
DOI: 10.1038/srep38399
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Funding
- University of Bristol
- EMBL
- EU Marie Curie Actions Cofund grant (EIPOD)
- postdoctoral EMBO fellowship [ALTF 900-2009]
- EC FP7 ComplexINC
- French Infrastructure for Integrated Structural Biology (FRISBI) [ANR-10-INSB-05-01]
- INSTRUCT as part of the European Strategy Forum on Research Infrastructures (ESFRI)
- BBSRC [BB/M003604/1, BB/I008675/1, BB/P000940/1]
- Wellcome Trust [103139, 092076, 108504]
- Methoden fur die Lebenswissenschaften' of the Baden-Wurttemberg Stiftung [Meth-P-LS-4]
- Agence Nationale de la Recherche [ANR-09-JCJC-0044]
- BBSRC [BB/I008675/1, BB/M003604/1, BB/P000940/1] Funding Source: UKRI
- Biotechnology and Biological Sciences Research Council [BB/M003604/1, BB/I008675/1] Funding Source: researchfish
- Agence Nationale de la Recherche (ANR) [ANR-09-JCJC-0044] Funding Source: Agence Nationale de la Recherche (ANR)
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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 super-complex. 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.
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