| Hauptseite > Publikationsdatenbank > A central cavity within the holo-translocon suggests a mechanism for membrane protein insertion > print |
| 001 | 825205 | ||
| 005 | 20210129225238.0 | ||
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| 100 | 1 | _ | |a Botte, Mathieu |0 P:(DE-HGF)0 |b 0 |
| 245 | _ | _ | |a A central cavity within the holo-translocon suggests a mechanism for membrane protein insertion |
| 260 | _ | _ | |a London |c 2016 |b Nature Publishing Group |
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| 520 | _ | _ | |a 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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| 773 | _ | _ | |a 10.1038/srep38399 |g Vol. 6, p. 38399 - |0 PERI:(DE-600)2615211-3 |p 38399 - |t Scientific reports |v 6 |y 2016 |x 2045-2322 |
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