التفاصيل البيبلوغرافية
| العنوان: |
COQ4 is required for the oxidative decarboxylation of the C1 carbon of coenzyme Q in eukaryotic cells. |
| المؤلفون: |
Pelosi, Ludovic1 (AUTHOR), Morbiato, Laura1,2,3 (AUTHOR), Burgardt, Arthur4 (AUTHOR), Tonello, Fiorella5 (AUTHOR), Bartlett, Abigail K.6,7 (AUTHOR), Guerra, Rachel M.7 (AUTHOR), Ferizhendi, Katayoun Kazemzadeh1 (AUTHOR), Desbats, Maria Andrea2,3 (AUTHOR), Rascalou, Bérengère1 (AUTHOR), Marchi, Marco2,3 (AUTHOR), Vázquez-Fonseca, Luis2,3 (AUTHOR), Agosto, Caterina8 (AUTHOR), Zanotti, Giuseppe9 (AUTHOR), Roger-Margueritat, Morgane1 (AUTHOR), Alcázar-Fabra, María10 (AUTHOR), García-Corzo, Laura10 (AUTHOR), Sánchez-Cuesta, Ana10 (AUTHOR), Navas, Plácido10 (AUTHOR), Brea-Calvo, Gloria10 (AUTHOR), Trevisson, Eva2,3 (AUTHOR) |
| المصدر: |
Molecular Cell. Mar2024, Vol. 84 Issue 5, p981-981. 1p. |
| مصطلحات موضوعية: |
*EUKARYOTIC cells, *DECARBOXYLATION, *CORYNEBACTERIUM glutamicum, *DECARBOXYLASES, *UBIQUINONES, *NAD (Coenzyme), *CELL physiology |
| مستخلص: |
Coenzyme Q (CoQ) is a redox lipid that fulfills critical functions in cellular bioenergetics and homeostasis. CoQ is synthesized by a multi-step pathway that involves several COQ proteins. Two steps of the eukaryotic pathway, the decarboxylation and hydroxylation of position C1, have remained uncharacterized. Here, we provide evidence that these two reactions occur in a single oxidative decarboxylation step catalyzed by COQ4. We demonstrate that COQ4 complements an Escherichia coli strain deficient for C1 decarboxylation and hydroxylation and that COQ4 displays oxidative decarboxylation activity in the non-CoQ producer Corynebacterium glutamicum. Overall, our results substantiate that COQ4 contributes to CoQ biosynthesis, not only via its previously proposed structural role but also via the oxidative decarboxylation of CoQ precursors. These findings fill a major gap in the knowledge of eukaryotic CoQ biosynthesis and shed light on the pathophysiology of human primary CoQ deficiency due to COQ4 mutations. [Display omitted] • The CoQ pathway is impaired at the decarboxylation step in COQ4-deficient human cells • COQ4-D164A has impaired metal binding and function but maintains complex Q • COQ4 functions as an oxidative decarboxylase in vivo • COQ4 is the missing enzyme that modifies C1 in the eukaryotic CoQ pathway Coenzyme Q, a redox lipid crucial for cellular bioenergetics and homeostasis, is synthesized by a multi-step pathway. Here, Pelosi et al. unveil the missing enzyme of the eukaryotic pathway by showing that COQ4 functions as an oxidative decarboxylase on the carbon 1 of coenzyme Q intermediates. [ABSTRACT FROM AUTHOR] |
| قاعدة البيانات: |
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