SHE9 deletion mutants display fitness defects during diauxic shift in Saccharomyces cerevisiae

Saccharomyces cerevisiae protein She9 is localized to the inner mitochondrial membrane and is required for normal mitochondrial morphology. While deletion mutants of SHE9 ( she9Δ ) are viable and display large ring-like mitochondrial structures, the molecular function of SHE9 is still unknown. We report a decreased growth of she9Δ cells during a diauxic shift, where mitochondria are primarily employing oxidative phosphorylation to generate ATP versus the alternative mechanism of glycolysis in high glucose conditions. Further bioinformatics analysis reveal putative functional protein associations, and proposes a model to aid in the understanding of the molecular function of She9.