期刊
CELL SYSTEMS
卷 6, 期 1, 页码 125-+出版社
CELL PRESS
DOI: 10.1016/j.cels.2017.11.012
关键词
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资金
- UW award
- NIH [R01GM112057, R01GM115591, P41GM108538, R01GM50942, R35GM118110]
- Department of Energy Great Lakes Bioenergy Research Center (Office of Science BER) [DE-FC02-07ER64494]
- NIH fellowship [T32GM008349]
- Wharton Scholar fellowship
- NIH Ruth L. Kirschstein NRSA [F30AG043282]
- Biochemistry Scholar fellowship
CoenzymeQ (CoQ) is a redox-active lipid required for mitochondrial oxidative phosphorylation (OxPhos). How CoQ biosynthesis is coordinated with the biogenesis of OxPhos protein complexes is unclear. Here, we show that the Saccharomyces cerevisiae RNA-binding protein (RBP) Puf3p regulates CoQ biosynthesis. To establish the mechanism for this regulation, we employed a multi-omic strategy to identify mRNAs that not only bind Puf3p but also are regulated by Puf3p in vivo. The CoQ biosynthesis enzyme Coq5p is a critical Puf3p target: Puf3p regulates the abundance of Coq5p and prevents its detrimental hyperaccumulation, thereby enabling efficient CoQ production. More broadly, Puf3p represses a specific set of proteins involved in mitochondrial protein import, translation, and OxPhos complex assembly (pathways essential to prime mitochondrial biogenesis). Our data reveal a mechanism for post-transcriptionally coordinating CoQ production with OxPhos biogenesis, and they demonstrate the power of multi-omics for defining genuine targets of RBPs.
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