期刊
BIOCHEMICAL JOURNAL
卷 443, 期 -, 页码 573-584出版社
PORTLAND PRESS LTD
DOI: 10.1042/BJ20111728
关键词
mitochondrion; messenger ribonucleoprotein particle (mRNP); oxidative phosphorylation (OXPHOS); translation; Y-box-binding protein-1 (YB-1)
资金
- Ministry of Education, Science, Technology, Sports and Culture of Japan [19209019, 21590337]
- Grants-in-Aid for Scientific Research [21590337, 22249018, 24659281, 19209019] Funding Source: KAKEN
Mitochondria play key roles in essential cellular functions, such as energy production, metabolic pathways and aging. Growth factor-mediated expression of the mitochondria] OXPHOS (oxidative phosphorylation) complex proteins has been proposed to play a fundamental role in metabolic homeostasis. Although protein translation is affected by general RNA-binding proteins, very little is known about the mechanism involved in mitochondrial OXPHOS protein translation. In the present study, serum stimulation induced nuclear-encoded OXPHOS protein expression, such as NDUFA9 [NADH dehydrogenase (ubiquinone) 1 alpha subcomplex, 9, 39 kDa], NDUFB8 [NADH dehydrogenase (ubiquinone) 1 beta subcomplex, 8, 19 kDa], SDHB [succinate dehydrogenase complex, subunit B, iron sulfur (Ip)] and UQCRFS1 (ubiquinol-cytochrome c reductase, Rieske iron sulfur polypeptide 1), and mitochondrial ATP production, in a translation-dependent manner. We also observed that the major ribonucleoprotein YB-1 (Y-box-binding protein-1) preferentially bound to these OXPHOS mRNAs and regulated the recruitment of mRNAs from inactive mRNPs (messenger ribonucleoprotein particles) to active polysomes. YB-1 depletion led to up-regulation of mitochondrial function through induction of OXPHOS protein translation from inactive mRNP release. In contrast, YB-1 overexpression suppressed the translation of these OXPHOS mRNAs through reduced polysome formation, suggesting that YB-1 regulated the translation of mitochondrial OXPHOS mRNAs through mRNA binding. Taken together, our findings suggest that YB-1 is a critical factor for translation that may control OXPHOS activity.
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