Dissecting structure and function of the monovalent cation/H⁺ antiporters Mdm38 and Ylh47 in Saccharomyces cerevisiae.

ABSTRACT: Saccharomyces cerevisiae Mdm38 and Ylh47 are homologs of the Ca²⁺/H⁺ antiporter Letm1, a candidate gene for seizures associated with Wolf-Hirschhorn syndrome in humans. Mdm38 is important for K⁺/H⁺ exchange across the inner mitochondrial membrane and contributes to membrane potential formation and mitochondrial protein translation. Ylh47 also localizes to the inner mitochondrial membrane. However, knowledge of the structures and detailed transport activities of Mdm38 and Ylh47 is limited. In this study, we conducted characterization of the ion transport activities and related structural properties of Mdm38 and Ylh47. Growth tests using Na⁺/H⁺ antiporter-deficient Escherichia coli strain TO114 showed that Mdm38

SUBMITTER: Tsujii M 

PROVIDER: S-EPMC11340316 | biostudies-literature | 2024 Aug

REPOSITORIES: biostudies-literature