Phosphorylation of the F(1)F(o) ATP synthase beta subunit: functional and structural consequences assessed in a model system.

ABSTRACT:

Rationale

We previously discovered several phosphorylations to the beta subunit of the mitochondrial F(1)F(o) ATP synthase complex in isolated rabbit myocytes on adenosine treatment, an agent that induces cardioprotection. The role of these phosphorylations is unknown.

Objective

The present study focuses on the functional consequences of phosphorylation of the ATP synthase complex beta subunit by generating nonphosphorylatable and phosphomimetic analogs in a model system, Saccharomyces cerevisiae.

Methods and results

The 4 amino acid residues with homology in yeast (T58, S213, T262, and T318) were studied with respect to growth, complex and supercomplex formation, and enzymatic activity (ATPase rate). The most striking mutant was the T262 site, for which the phosphomi

SUBMITTER: Kane LA 

PROVIDER: S-EPMC2835499 | biostudies-literature | 2010 Feb

REPOSITORIES: biostudies-literature