Cardiolipin binding enhances KcsA channel gating via both its specific and dianion-monoanion interchangeable sites.

ABSTRACT: KcsA is a potassium channel with a plethora of structural and functional information, but its activity in the KcsA-producing actinomycete membranes remains elusive. To determine lipid species involved in channel-modulation, a surface plasmon resonance (SPR)-based methodology, characterized by immobilization of membrane proteins under a membrane environment, was applied. Dianionic cardiolipin (CL) showed extremely higher affinity for KcsA than monoanionic lipids. The SPR experiments further demonstrated that CL bound not only to the N-terminal M0 helix, a lipid-sensor domain, but to the M0 helix-deleted mutant. In contrast, monoanionic lipids interacted primarily with the M0 helix. This indicates the presence of an alternative CL-binding site, plausibly in the transmembrane domain. Single-c

SUBMITTER: Iwamoto M 

PROVIDER: S-EPMC10709135 | biostudies-literature | 2023 Dec

REPOSITORIES: biostudies-literature