Acetyl coenzyme A, a key intermediate of the mitochondrial carbon metabolism, is formed by the mitochondrial pyruvate dehydrogenase complex (PDC). The dihydrolipoamide dehydrogenase Lpd1 is a catalytic component of PDC. Lpd1 has been recovered during 2D-PAGE screening for the hypha-specific proteins in Candida albicans. The Lpd1 protein, as visualized by a GFP-fusion, was localized in the mitochondria during the logarithmic yeast growth and the filamentous growth. The GFP signal was prevalent and relatively uniform toward the tip of the hyphae. The functions of the LPD1 gene were investigated by construction of lpd1/lpd1 mutant strain. This homozygous deletion mutant was unable to grow on non-fermentable carbon sources including glycerol, ethanol, acetate, and citrate. In addition, the lpd1/lpd1 strain exhibited a slow-growth phenotype on glucose-containing media and a marked sensitivity to 0.5mM of hydrogen peroxide. LPD1 was shown to be required for filamentous growth under a serum-containing hyphal-inducing condition. These results suggest a possible relationship between mitochondrial respiration and filamentous growth.
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