Identification of an amphipathic peptide sensor of the Bacillus subtilis fluid membrane microdomains.

ABSTRACT: Regions of increased fluidity are newly found bacterial membrane microdomains that are composed of short, unsaturated and branched fatty acyl chains in a fluid and disordered state. Currently, little is known about how proteins are recruited and localized to these membrane domains. Here, we identify a short amphipathic α-peptide in a previously unreported crystal structure and show that it is responsible for peripheral localization of the phosphate acyltransferase PlsX to the fluid microdomains in Bacillus subtilis. Mutations disrupting the amphipathic interaction or increasing the nonpolar interaction are found to redistribute the protein to the cytosol or other part of the plasma membrane, causing growth defects. These results reveal a mechanism of peripheral membrane sensing thro

SUBMITTER: Jiang Y 

PROVIDER: S-EPMC6702220 | biostudies-literature | 2019

REPOSITORIES: biostudies-literature