![]() ![]() (D) Subcellular localization of Fmp12-yeGFP by fluorescent GAPDH and porin were analyzed as controls of cytoplasmicĪnd mitochondrial proteins, respectively. TheĪrrow indicates the predicted size of Fmp12-3HA truncated at itsĪmino-terminal MTS. The cells without or with expression of Fmp12-3HA from pVV209-FMP12. (C) Detection of Fmp12-3HA in the whole cell extract (WCE) and PVV209-FMP12) on SD, SD-N-C+Pro, and SD-N-C+Glu media. PVV209) or overexpressing FMP12 (pVV208-FMP12, Or BY4741u Δ fmp12 cells harboring the empty vector (pVV208, Wild-type strain (BY4741) and its deletion mutants on SD, SD-N-C+Pro, The function of Fmp12, which has a similarity with α-ketoglutarate-dependent dioxygenases of the yeast Candida species and human, might inhibit cell growth by skipping the ATP production step of the TCA cycle.įmp12 carbon source mitochondria proline yeast Saccharomyces cerevisiae α-ketoglutarate-dependent dioxygenase. These results provided the first evidence that proline can be utilized as a carbon source via the mitochondrial proline metabolic pathway and the subsequent tricarboxylic acid (TCA) cycle in S. Deletion of the genes that encode mitochondrial enzymes, such as proline dehydrogenase ( PUT1), Δ 1-pyrroline-5-carboxylate dehydrogenase ( PUT2), alanine transaminase ( ALT1), and α-ketoglutarate dehydrogenase subunit ( KGD1), abolished the enhanced cell growth in Δ fmp12. The Fmp12 protein was localized in the mitochondria and was constitutively expressed. ![]() In contrast, overexpression of FMP12 negatively affected cell growth under the same condition. ![]() In the process of study on the physiological roles of the found-in-mitochondrial-proteome ( FMP) genes in proline metabolism, we found that Δ fmp12 cells could grow better than wild-type cells on agar plate medium containing proline as the sole nitrogen and carbon sources. cerevisiae cells has not been studied yet. However, utilization of proline as a carbon source in S. The amino acid proline functions as a nitrogen source and as a stress protectant in the yeast Saccharomyces cerevisiae. ![]()
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