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Unsaturated fatty acids augment protein transport via the SecA:SecYEG translocon
Author(s) -
Kamel Michael,
Löwe Maryna,
SchottVerdugo Stephan,
Gohlke Holger,
Kedrov Alexej
Publication year - 2022
Publication title -
the febs journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.981
H-Index - 204
eISSN - 1742-4658
pISSN - 1742-464X
DOI - 10.1111/febs.16140
Subject(s) - translocon , secretion , cardiolipin , biochemistry , biology , chromosomal translocation , cytoplasm , fatty acid , transport protein , secretory protein , protein folding , phospholipid , biophysics , microbiology and biotechnology , membrane protein , membrane , gene
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.