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We would like to thank Ladislav Kovac and Jordan Kolarov (Comenius University in Bratislava) for stimulating discussions and support, Johannes H. Hegemann (Heinrich-Heine-Universitat, Dusseldorf, Germany) for the plasmid pUG36, and Geraldine Butler (University College Dublin, Ireland) for the C. parapsilosis strain CDUl. We acknowledge the technical support of the sequencing core facility at the Centre for Genomic Regulation. This work was supported by the Slovak grant agency (VEGA) (1/0333/15 and 1/0052/16) and the Slovak Research and Development Agency (APVV) (14-0253 and 15-0022). The T.G. group is supported in part by a grant from the Spanish ministry of Economy and Competitiveness (BI02012-37161), a grant from the Qatar National Research Fund (NPRP 5-298-3-086), and a grant from the European Research Council (ERC) under the European Union's Seventh Framework Program (FP/2007-2013)/ERC (grant agreement no. ERC-2012-StG-310325).
Mitochondrial Carriers Link the Catabolism of Hydroxyaromatic Compounds to the Central Metabolism in Candida parapsilosis
Publicated to:G3-Genes Genomes Genetics. 6 (12): 4047-4058 - 2016-12-01 6(12), DOI: 10.1534/g3.116.034389
Authors: Zeman, I; Nebohácová, M; Gérecová, G; Katonová, K; Jánosíková, E; Jakúbková, M; Centárová, I; Duncková, I; Tomáska, L; Pryszcz, LP; Gabaldón, T; Nosek, J
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Abstract
The pathogenic yeast Candida parapsilosis metabolizes hydroxyderivatives of benzene and benzoic acid to compounds channeled into central metabolism, including the mitochondrially localized tricarboxylic acid cycle, via the 3-oxoadipate and gentisate pathways. The orchestration of both catabolic pathways with mitochondrial metabolism as well as their evolutionary origin is not fully understood. Our results show that the enzymes involved in these two pathways operate in the cytoplasm with the exception of the mitochondrially targeted 3-oxoadipate CoA-transferase (Osc1p) and 3-oxoadipyl-CoA thiolase (Oct1p) catalyzing the last two reactions of the 3-oxoadipate pathway. The cellular localization of the enzymes indicates that degradation of hydroxyaromatic compounds requires a shuttling of intermediates, cofactors, and products of the corresponding biochemical reactions between cytosol and mitochondria. Indeed, we found that yeast cells assimilating hydroxybenzoates increase the expression of genes SFC1, LEU5, YHM2, and MPC1 coding for succinate/fumarate carrier, coenzyme A carrier, oxoglutarate/citrate carrier, and the subunit of pyruvate carrier, respectively. A phylogenetic analysis uncovered distinct evolutionary trajectories for sparsely distributed gene clusters coding for enzymes of both pathways. Whereas the 3-oxoadipate pathway appears to have evolved by vertical descent combined with multiple losses, the gentisate pathway shows a striking pattern suggestive of horizontal gene transfer to the evolutionarily distant Mucorales.
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The work has been published in the journal G3-Genes Genomes Genetics due to its progression and the good impact it has achieved in recent years, according to the agency Scopus (SJR), it has become a reference in its field. In the year of publication of the work, 2016, it was in position , thus managing to position itself as a Q1 (Primer Cuartil), in the category Medicine (Miscellaneous). Notably, the journal is positioned above the 90th percentile.
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Según las diferentes agencias de indexación, el número de citas acumuladas por esta publicación hasta la fecha 2025-07-25:
- WoS: 7
- Scopus: 5
- Europe PMC: 4
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This work has been carried out with international collaboration, specifically with researchers from: Austria; Poland; Slovakia.