Specific cardiolipin-SecY interactions are required for proton-motive force stimulation of protein secretion.

ABSTRACT: The transport of proteins across or into membranes is a vital biological process, achieved in every cell by the conserved Sec machinery. In bacteria, SecYEG combines with the SecA motor protein for secretion of preproteins across the plasma membrane, powered by ATP hydrolysis and the transmembrane proton-motive force (PMF). The activities of SecYEG and SecA are modulated by membrane lipids, particularly cardiolipin (CL), a specialized phospholipid known to associate with a range of energy-transducing machines. Here, we identify two specific CL binding sites on the Thermotoga maritima SecA-SecYEG complex, through application of coarse-grained molecular dynamics simulations. We validate the computational data and demonstrate the conserved nature of the binding sites using in vitro mut

SUBMITTER: Corey RA 

PROVIDER: S-EPMC6077702 | biostudies-literature | 2018 Jul

REPOSITORIES: biostudies-literature