Journal Article

FZJ-2016-07676

http://join2-wiki.gsi.de/foswiki/pub/Main/Artwork/join2_logo100x88.png A central cavity within the holo-translocon suggests a mechanism for membrane protein insertion

Botte, M. ; Zaccai, N. R. ; Nijeholt, J. L. à. ; Martin, R. ; Knoops, K. ; Papai, G. ; Zou, J. ; Deniaud, A. ; Karuppasamy, M. ; Jiang, Q. ; Roy, A. S. ; Schulten, K. ; Schultz, P. ; Rappsilber, J. ; Zaccai, G. ; Berger, I. ; Collinson, I. (Corresponding author) ; Schaffitzel, C. (Corresponding author)

2016
Nature Publishing Group London

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Please use a persistent id in citations: http://hdl.handle.net/2128/13412  doi:10.1038/srep38399

Abstract: 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.

Keyword(s): Health and Life (1st) ; Biology (2nd)

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Contributing Institute(s):

1. JCNS-FRM-II (JCNS (München) ; Jülich Centre for Neutron Science JCNS (München) ; JCNS-FRM-II)

Research Program(s):

1. 6G15 - FRM II / MLZ (POF3-6G15) (POF3-6G15)
2. 6G4 - Jülich Centre for Neutron Research (JCNS) (POF3-623) (POF3-623)

Experiment(s):

1. KWS-2: Small angle scattering diffractometer (NL3ao)

Appears in the scientific report 2016

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