Directly light-regulated binding of RGS-LOV photoreceptors to anionic membrane phospholipids.

ABSTRACT: We report natural light-oxygen-voltage (LOV) photoreceptors with a blue light-switched, high-affinity (K_D ∼ 10^-7 M), and direct electrostatic interaction with anionic phospholipids. Membrane localization of one such photoreceptor, BcLOV4 from Botrytis cinerea, is directly coupled to its flavin photocycle, and is mediated by a polybasic amphipathic helix in the linker region between the LOV sensor and its C-terminal domain of unknown function (DUF), as revealed through a combination of bioinformatics, computational protein modeling, structure-function studies, and optogenetic assays in yeast and mammalian cell line expression systems. In model systems, BcLOV4 rapidly translocates from the cytosol to plasma membrane (∼1 second). The reversible electrostati

SUBMITTER: Glantz ST 

PROVIDER: S-EPMC6099885 | biostudies-literature | 2018 Aug

REPOSITORIES: biostudies-literature