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language
eng
Author
Nishida, Ikuhisa Department of Life Sciences, Faculty of Life and Environmental Sciences, Shimane University, Matsue, Japan
Yanai, Ryota Department of Life Sciences, Faculty of Life and Environmental Sciences, Shimane University, Matsue, Japan
Kaino, Tomohiro Department of Life Sciences, Faculty of Life and Environmental Sciences, Shimane University, Matsue, Japan
Description
Coenzyme Q (CoQ, ubiquinone) is an essential component of the electron transport system in aerobic organisms. Human type CoQ10, which has 10 units of isoprene in its quinone structure, is especially valuable as a food supplement. Therefore, studying the biosynthesis of CoQ10 is important not only for increasing metabolic knowledge, but also for improving biotechnological production. Herein, we show that Schizosaccharomyces pombe utilizes p-aminobenzoate (PABA) in addition to p-hydroxybenzoate (PHB) as a precursor for CoQ10 synthesis. We explored compounds that affect the synthesis of CoQ10 and found benzoic acid (Bz) at >5 μg/mL inhibited CoQ biosynthesis without accumulation of apparent CoQ intermediates. This inhibition was counteracted by incubation with a 10-fold lower amount of PABA or PHB. Overexpression of PHB-polyprenyl transferase encoded by ppt1 (coq2) also overcame the inhibition of CoQ biosynthesis by Bz. Inhibition by Bz was efficient in S. pombe and Schizosaccharomyces japonicus, but less so in Saccharomyces cerevisiae, Aureobasidium pullulans, and Escherichia coli. Bz also inhibited a S. pombe ppt1 (coq2) deletion strain expressing human COQ2, and this strain also utilized PABA as a precursor of CoQ10. Thus, Bz is likely to inhibit prenylation reactions involving PHB or PABA catalyzed by Coq2.
Journal Title
PLoS ONE
Volume
15
Issue
11
ISSN
1932-6203
Published Date
2020-11-24
DOI
Publisher
Public Library of Science
NII Type
Journal Article
Format
PDF
Text Version
出版社版
OAI-PMH Set
Faculty of Life and Environmental Science
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