The second respiratory chain of Candida parapsilosis: a comprehensive study
Abstract
The yeast C. parapsilosis CBS7157 is strictly dependent on oxidative metabolism for growth since it lacks a fermentative pathway. It is nevertheless able to grow on high glucose concentrations and also on a glycerol medium supplemented with antimycin A or drugs acting at the level of mitochondrial protein synthesis. Besides its normal respiratory chain C. parapsilosis develops a second electron transfer chain antimycin A-insensitive which allows the oxidation of cytoplasmic NAD(P)H resulting from glycolytic and hexose monophosphate pathways functioning through a route different from the NADH-coenzyme Q oxidoreductase described in S. cerevisiae or from the alternative pathways described in numerous plants and microorganisms. The second respiratory chain of C. parapsilosis involves 2 dehydrogenases specific for NADH and NADPH respectively, which are amytal and mersalyl sensitive and located on the outer face of the inner membrane. Since this antimycin A-insensitive pathway is fully inhibited by myxothiazol, it was hypothesized that electrons are transferred to a quinone pool that is different from the classical coenzyme Q-cytochrome b cycle. Two inhibitory sites were evidenced with myxothiazol, one related to the classical pathway, the other to the second pathway and thus, the second quinone pool could bind to a Q-binding protein at a specific site. Elimination of this second pool leads to a fully antimycin A-sensitive NADH oxidation, whereas its reincorporation in mitochondria…
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Higher aa3 cytochrome levels could suggest induction of the PAR pathway and activation of additional cytochrome pools.
“which could suggest induction of the PAR pathway and activation of additional cytochrome pools, previously reported in Candida parapsilosis and C. albicans (Guerin et al. 1989; Ruy et al. 2006).”
From <i>Candida albicans</i> PPR proteins are required for the expression of respiratory Complex I subunits (2024) · cites this paper as Guerin et al. 1989
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- Authors
- Guerin, M., Camougrand, N., Caubet, R., Zniber, S., Velours, G., Manon, S., Guelin, E., & Cheyrou, A.
- Affiliations
- Centre National de la Recherche Scientifique (FR)
- ORCID
- Camougrand, Nadine
- Venue
- Biochimie
- Publisher
- Elsevier BV
- Published
- 1989-08
- Volume
- 71
- Issue
- 8
- Pages
- 887-902
- ISSN
- 0037-9042 (ISSN-L)
- 0300-9084
- OpenAlex
- W2094118636
- Cited by
- 23
- References
- 43
- Citations by year
- 2025: 1 · 2024: 1 · 2021: 1 · 2020: 1 · 2017: 1 · 2015: 1
- FWCI
- 0.64
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- Biochimie (publishedVersion)
- PubMed (publishedVersion)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Mitochondrial Function and Pathology
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Fungal and yeast genetics research
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Coenzyme Q10 studies and effects
- Keywords
- Candida parapsilosis, NADH oxidation, NADPH dehydrogenase, myxothiazol, quinone pool, cytochrome c, alternative oxidase, oxidative phosphorylation, yeast mitochondria, glycolysis, hexose monophosphate pathway, cytochrome bc1 complex
- MeSH terms
- Candida, Cytochromes, Drug Resistance, Microbial, Electron Transport, Mitochondria, NADP, Phosphorylation, Saccharomyces cerevisiae
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