TY  - JOUR
AU  - Kamel, Michael
AU  - Löwe, Maryna
AU  - Schott-Verdugo, Stephan
AU  - Gohlke, Holger
AU  - Kedrov, Alexej
TI  - Unsaturated fatty acids augment protein transport via the SecA:SecYEG translocon
JO  - The FEBS journal
VL  - 289
IS  - 1
SN  - 1742-4658
CY  - Oxford [u.a.]
PB  - Wiley-Blackwell
M1  - FZJ-2021-03306
SP  - 140-162
PY  - 2022
AB  - The translocon SecYEG and the associated ATPase SecA form the primary protein secretion system in the cytoplasmic membrane of bacteria. The secretion is essentially dependent on the surrounding lipids, but the mechanistic understanding of their role in SecA : SecYEG activity is sparse. Here, we reveal that the unsaturated fatty acids (UFAs) of the membrane phospholipids, including tetraoleoyl-cardiolipin, stimulate SecA : SecYEG-mediated protein translocation up to ten-fold. Biophysical analysis and molecular dynamics simulations show that UFAs increase the area per lipid and cause loose packing of lipid head groups, where the N-terminal amphipathic helix of SecA docks. While UFAs do not affect the translocon folding, they promote SecA binding to the membrane, and the effect is enhanced up to fivefold at elevated ionic strength. Tight SecA : lipid interactions convert into the augmented translocation. Our results identify the fatty acid structure as a notable factor in SecA : SecYEG activity, which may be crucial for protein secretion in bacteria, which actively change their membrane composition in response to their habitat.
LB  - PUB:(DE-HGF)16
C6  - pmid:34312977
UR  - <Go to ISI:>//WOS:000682136100001
DO  - DOI:10.1111/febs.16140
UR  - https://juser.fz-juelich.de/record/894605
ER  -