TY  - JOUR
AU  - Martin, Remy
AU  - Larsen, Andreas Haahr
AU  - Corey, Robin Adam
AU  - Midtgaard, Søren Roi
AU  - Frielinghaus, Henrich
AU  - Schaffitzel, Christiane
AU  - Arleth, Lise
AU  - Collinson, Ian
TI  - Structure and Dynamics of the Central Lipid Pool and Proteins of the Bacterial Holo-Translocon
JO  - Biophysical journal
VL  - 116
IS  - 10
SN  - 0006-3495
CY  - Bethesda, Md.
PB  - Soc.
M1  - FZJ-2019-03831
SP  - 1931 - 1940
PY  - 2019
AB  - The bacterial Sec translocon, SecYEG, associates with accessory proteins YidC and the SecDF-YajC subcom-plex to form the bacterial holo-translocon (HTL). The HTL is a dynamic and flexible protein transport machine capable of coor-dinating protein secretion across the membrane and efficient lateral insertion of nascent membrane proteins. It has been hypothesized that a central lipid core facilitates the controlled passage of membrane proteins into the bilayer, ensuring the efficient formation of their native state. By performing small-angle neutron scattering on protein solubilized in ‘‘match-out’’ deuterated detergent, we have been able to interrogate a ‘‘naked’’ HTL complex, with the scattering contribution of the sur-rounding detergent micelle rendered invisible. Such an approach has allowed the confirmation of a lipid core within the HTL, which accommodates between 8 and 29 lipids. Coarse-grained molecular dynamics simulations of the HTL also demon-strate a dynamic, central pool of lipids. An opening at this lipid-rich region between YidC and the SecY lateral gate may provide an exit gateway for newly synthesized, correctly oriented, membrane protein helices, or even small bundles of helices, to emerge from the HTL.
LB  - PUB:(DE-HGF)16
C6  - pmid:31053257
UR  - <Go to ISI:>//WOS:000468419300015
DO  - DOI:10.1016/j.bpj.2019.04.002
UR  - https://juser.fz-juelich.de/record/863860
ER  -