1. The mitochondrial protein Mcu1 plays important roles in carbon source utilization, filamentation, and virulence in Candida albicans
- Author
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Li Tao, James B. Konopka, Haitao Wang, Chengjun Cao, Yue Wang, Weihong Liang, Guobo Guan, Shamoon Naseem, and Guanghua Huang
- Subjects
Mutant ,Hyphae ,Virulence ,Biology ,Microbiology ,Acetylglucosamine ,Fungal Proteins ,Mitochondrial Proteins ,Mice ,Candida albicans ,Genetics ,Animals ,Amino Acids ,Gene ,Pathogen ,chemistry.chemical_classification ,Candidemia ,Metabolism ,biology.organism_classification ,Carbon ,Corpus albicans ,Amino acid ,Disease Models, Animal ,chemistry ,Biochemistry ,Multigene Family ,Gene Deletion - Abstract
The fungus Candida albicans is both a pathogen and a commensal in humans. The ability to utilize different carbon sources available in diverse host niches is vital for both commensalism and pathogenicity. N-acetylglucosamine (GlcNAc) is an important signaling molecule as well as a carbon source in C. albicans. Here, we report the discovery of a novel gene MCU1 essential for GlcNAc utilization. Mcu1 is located in mitochondria and associated with multiple energy- and metabolism-related proteins including Por1, Atp1, Pet9, and Mdh1. Consistently, inactivating Por1 impaired GlcNAc utilization as well. Deletion of MCU1 also caused defects in utilizing non-fermentable carbon sources and amino acids. Furthermore, MCU1 is required for filamentation in several inducing conditions and virulence in a mouse systemic infection model. We also deleted TGL99 and GUP1, two genes adjacent to MCU1, and found that the gup1/gup1 mutant exhibited mild defects in the utilization of several carbon sources including GlcNAc, maltose, galactose, amino acids, and ethanol. Our results indicate that MCU1 exists in a cluster of genes involved in the metabolism of carbon sources. Given its importance in metabolism and lack of a homolog in humans, Mcu1 could be a potential target for developing antifungal agents.
- Published
- 2015
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