Analysis of Arabidopsis TPK2 and KCO3 reveals structural properties required for K⁺ channel function.

ABSTRACT: Arabidopsis thaliana contains five tandem-pore domain potassium channels, TPK1-TPK5 and the related one-pore domain potassium channel, KCO3. Although KCO3 is unlikely to be an active channel, it still has a physiological role in plant cells. TPK2 is most similar to KCO3 and both are localized to the tonoplast. However, their function remains poorly understood. Here, taking advantage of the similarities between TPK2 and KCO3, we evaluated Ca²⁺ binding to the EF hands in TPK2, and the elements of KCO3 required for K⁺ channel activity. Presence of both EF-hand motifs in TPK2 resulted in Ca²⁺ binding, but EF1 or EF2 alone failed to interact with Ca²⁺. The EF hands were not required for K⁺ transport activity. EF1 contains two cysteines sepa

SUBMITTER: Uehara C 

PROVIDER: S-EPMC7757853 | biostudies-literature | 2020 Dec

REPOSITORIES: biostudies-literature