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A unique flavoenzyme operates in ubiquinone biosynthesis in photosynthesis-related eukaryotes
Coenzyme Q (CoQ) is an electron transporter in the mitochondrial respiratory chain, yet the biosynthetic pathway in eukaryotes remains only partially resolved. C6-hydroxylation completes the benzoquinone ring full substitution, a hallmark of CoQ. Here, we show that plants use a unique flavin-depende...
Autores principales: | , , , , , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
American Association for the Advancement of Science
2021
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8654299/ https://www.ncbi.nlm.nih.gov/pubmed/34878842 http://dx.doi.org/10.1126/sciadv.abl3594 |
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author | Xu, Jing-Jing Zhang, Xiao-Fan Jiang, Yan Fan, Hang Li, Jian-Xu Li, Chen-Yi Zhao, Qing Yang, Lei Hu, Yong-Hong Martin, Cathie Chen, Xiao-Ya |
author_facet | Xu, Jing-Jing Zhang, Xiao-Fan Jiang, Yan Fan, Hang Li, Jian-Xu Li, Chen-Yi Zhao, Qing Yang, Lei Hu, Yong-Hong Martin, Cathie Chen, Xiao-Ya |
author_sort | Xu, Jing-Jing |
collection | PubMed |
description | Coenzyme Q (CoQ) is an electron transporter in the mitochondrial respiratory chain, yet the biosynthetic pathway in eukaryotes remains only partially resolved. C6-hydroxylation completes the benzoquinone ring full substitution, a hallmark of CoQ. Here, we show that plants use a unique flavin-dependent monooxygenase (CoqF), instead of di-iron enzyme (Coq7) operating in animals and fungi, as a C6-hydroxylase. CoqF evolved early in eukaryotes and became widely distributed in photosynthetic and related organisms ranging from plants, algae, apicomplexans, and euglenids. Independent alternative gene losses in different groups and lateral gene transfer have ramified CoqF across the eukaryotic tree with predominance in green lineages. The exclusive presence of CoqF in Streptophyta hints at an association of the flavoenzyme with photoautotrophy in terrestrial environments. CoqF provides a phylogenetic marker distinguishing eukaryotes and represents a previously unknown target for drug design against parasitic protists. |
format | Online Article Text |
id | pubmed-8654299 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2021 |
publisher | American Association for the Advancement of Science |
record_format | MEDLINE/PubMed |
spelling | pubmed-86542992021-12-16 A unique flavoenzyme operates in ubiquinone biosynthesis in photosynthesis-related eukaryotes Xu, Jing-Jing Zhang, Xiao-Fan Jiang, Yan Fan, Hang Li, Jian-Xu Li, Chen-Yi Zhao, Qing Yang, Lei Hu, Yong-Hong Martin, Cathie Chen, Xiao-Ya Sci Adv Biomedicine and Life Sciences Coenzyme Q (CoQ) is an electron transporter in the mitochondrial respiratory chain, yet the biosynthetic pathway in eukaryotes remains only partially resolved. C6-hydroxylation completes the benzoquinone ring full substitution, a hallmark of CoQ. Here, we show that plants use a unique flavin-dependent monooxygenase (CoqF), instead of di-iron enzyme (Coq7) operating in animals and fungi, as a C6-hydroxylase. CoqF evolved early in eukaryotes and became widely distributed in photosynthetic and related organisms ranging from plants, algae, apicomplexans, and euglenids. Independent alternative gene losses in different groups and lateral gene transfer have ramified CoqF across the eukaryotic tree with predominance in green lineages. The exclusive presence of CoqF in Streptophyta hints at an association of the flavoenzyme with photoautotrophy in terrestrial environments. CoqF provides a phylogenetic marker distinguishing eukaryotes and represents a previously unknown target for drug design against parasitic protists. American Association for the Advancement of Science 2021-12-08 /pmc/articles/PMC8654299/ /pubmed/34878842 http://dx.doi.org/10.1126/sciadv.abl3594 Text en Copyright © 2021 The Authors, some rights reserved; exclusive licensee American Association for the Advancement of Science. No claim to original U.S. Government Works. Distributed under a Creative Commons Attribution NonCommercial License 4.0 (CC BY-NC). https://creativecommons.org/licenses/by-nc/4.0/This is an open-access article distributed under the terms of the Creative Commons Attribution-NonCommercial license (https://creativecommons.org/licenses/by-nc/4.0/) , which permits use, distribution, and reproduction in any medium, so long as the resultant use is not for commercial advantage and provided the original work is properly cited. |
spellingShingle | Biomedicine and Life Sciences Xu, Jing-Jing Zhang, Xiao-Fan Jiang, Yan Fan, Hang Li, Jian-Xu Li, Chen-Yi Zhao, Qing Yang, Lei Hu, Yong-Hong Martin, Cathie Chen, Xiao-Ya A unique flavoenzyme operates in ubiquinone biosynthesis in photosynthesis-related eukaryotes |
title | A unique flavoenzyme operates in ubiquinone biosynthesis in photosynthesis-related eukaryotes |
title_full | A unique flavoenzyme operates in ubiquinone biosynthesis in photosynthesis-related eukaryotes |
title_fullStr | A unique flavoenzyme operates in ubiquinone biosynthesis in photosynthesis-related eukaryotes |
title_full_unstemmed | A unique flavoenzyme operates in ubiquinone biosynthesis in photosynthesis-related eukaryotes |
title_short | A unique flavoenzyme operates in ubiquinone biosynthesis in photosynthesis-related eukaryotes |
title_sort | unique flavoenzyme operates in ubiquinone biosynthesis in photosynthesis-related eukaryotes |
topic | Biomedicine and Life Sciences |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8654299/ https://www.ncbi.nlm.nih.gov/pubmed/34878842 http://dx.doi.org/10.1126/sciadv.abl3594 |
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