ArticleThe Biochemical journal2014
Comparisons of subunit 5A and 5B isoenzymes of yeast cytochrome c oxidase.
Article in The Biochemical journal, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
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Who cites it
9 citing papers in PubMed, 20 citations in OpenAlex.
- Approach of a small protein to the biomimetic bis-(μ-oxo) dicopper active-site installed in MOF-808 pores with restricted access perturbs substrate selectivity of oxidase nanozyme.Chemical science · 2024Article
- Translational activators and mitoribosomal isoforms cooperate to mediate mRNA-specific translation in Schizosaccharomyces pombe mitochondria.Nucleic acids research · 2021Article
- Structure and Mechanism of Respiratory III-IV Supercomplexes in Bioenergetic Membranes.Chemical reviews · 2021Review
- NMR structural analysis of the yeast cytochrome c oxidase subunit Cox13 and its interaction with ATP.BMC biology · 2021Article
- Cryo-EM structure and kinetics reveal electron transfer by 2D diffusion of cytochromeProceedings of the National Academy of Sciences of the United States of America · 2021Article
- Electron Transfer Coupled to Conformational Dynamics in Cell Respiration.Frontiers in molecular biosciences · 2021Article
- Rcf2 revealed in cryo-EM structures of hypoxic isoforms of mature mitochondrial III-IV supercomplexes.Proceedings of the National Academy of Sciences of the United States of America · 2020Article
- Structure of yeast cytochrome c oxidase in a supercomplex with cytochrome bcNature structural & molecular biology · 2019Article
- Tissue- and Condition-Specific Isoforms of Mammalian CytochromeOxidative medicine and cellular longevity · 2017Review
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
Abstract
Subunit 5 of Saccharomyces cerevisiae cytochrome c oxidase (CcO) is essential for assembly and has two isoforms, 5A and 5B. 5A is expressed under normoxic conditions, whereas 5B is expressed at very low oxygen tensions. As a consequence, COX5A-deleted strains (Δcox5A) have no or only low levels of CcO under normoxic conditions rendering them respiratory deficient. Previous studies have reported that respiratory growth could be restored by combining Δcox5A with mutations of ROX1 that encodes a repressor of COX5B expression. In these mutants, 5B isoenzyme expression level was 30-50% of wild-type (5A isoenzyme) and exhibited a maximum catalytic activity up to 3-fold faster than that of 5A isoenzyme. To investigate the origin of this effect, we constructed a mutant strain in which COX5B replaced COX5A downstream of the COX5A promoter. This strain expressed wild-type levels of the 5B isoenzyme, without the complication of additional effects caused by mutation of ROX1. When produced this way, the isoenzymes displayed no significant differences in their maximum catalytic activities or in their affinities for oxygen or cytochrome c. Hence the elevated activity of the 5B isoenzyme in the rox1 mutant is not caused simply by exchange of isoforms and must arise from an additional effect that remains to be resolved.
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