TY - JOUR
AU - Botte, Mathieu
AU - Zaccai, Nathan R.
AU - Nijeholt, Jelger Lycklama à.
AU - Martin, Remy
AU - Knoops, Kèvin
AU - Papai, Gabor
AU - Zou, Juan
AU - Deniaud, Aurélien
AU - Karuppasamy, Manikandan
AU - Jiang, Qiyang
AU - Roy, Abhishek Singha
AU - Schulten, Klaus
AU - Schultz, Patrick
AU - Rappsilber, Juri
AU - Zaccai, Giuseppe
AU - Berger, Imre
AU - Collinson, Ian
AU - Schaffitzel, Christiane
TI - A central cavity within the holo-translocon suggests a mechanism for membrane protein insertion
JO - Scientific reports
VL - 6
SN - 2045-2322
CY - London
PB - Nature Publishing Group
M1 - FZJ-2016-07676
SP - 38399 -
PY - 2016
AB - 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.
LB - PUB:(DE-HGF)16
UR - <Go to ISI:>//WOS:000389740800001
C6 - pmid:27924919
DO - DOI:10.1038/srep38399
UR - https://juser.fz-juelich.de/record/825205
ER -