%0 Journal Article
%A Botte, Mathieu
%A Zaccai, Nathan R.
%A Nijeholt, Jelger Lycklama à.
%A Martin, Remy
%A Knoops, Kèvin
%A Papai, Gabor
%A Zou, Juan
%A Deniaud, Aurélien
%A Karuppasamy, Manikandan
%A Jiang, Qiyang
%A Roy, Abhishek Singha
%A Schulten, Klaus
%A Schultz, Patrick
%A Rappsilber, Juri
%A Zaccai, Giuseppe
%A Berger, Imre
%A Collinson, Ian
%A Schaffitzel, Christiane
%T A central cavity within the holo-translocon suggests a mechanism for membrane protein insertion
%J Scientific reports
%V 6
%@ 2045-2322
%C London
%I Nature Publishing Group
%M FZJ-2016-07676
%P 38399 -
%D 2016
%X 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.
%F PUB:(DE-HGF)16
%9 Journal Article
%U <Go to ISI:>//WOS:000389740800001
%$ pmid:27924919
%R 10.1038/srep38399
%U https://juser.fz-juelich.de/record/825205