期刊
SCIENCE CHINA-LIFE SCIENCES
卷 65, 期 2, 页码 227-235出版社
SCIENCE PRESS
DOI: 10.1007/s11427-021-1962-0
关键词
mitochondria; OPA1; chaperone; mitochondrial homeostasis; heat shock
类别
资金
- National Key Research and Development Program of China [2017YFA0106300, 2017YFA0102900, 2019YFA09004500, 2017YFC1001602, 2016YFA0100300, 2018YFA0107100]
- Strategic Priority Research Program of the Chinese Academy of Sciences [XDA16030505]
- National Natural Science Foundation of China [32025010, 31801168, 31900614, 31970709, 81901275, 32070729]
- Key Research Program of Frontier Sciences, CAS [QYZDB-SSW-SMC001]
- International Cooperation Program, CAS [154144KYSB20200006]
- Guangdong Province Science and Technology Program [2020B1212060052, 2018A030313825, 2018GZR110103002, 2020A1515011200, 2020A1515010919, 2020A1515011410, 2021A1515012513]
- Guangzhou Science and Technology Program [201807010067, 202002030277, 202102021250, 202102020827, 202102080066]
- CAS Youth Innovation Promotion Association
Our study showed that S-OPA1 acts as a molecular chaperone in the intermembrane space (IMS) of mitochondria, protecting substrate proteins from aggregation and enhancing thermotolerance in E. coli. S-OPA1 also confers thermotolerance on IMS proteins such as neurolysin, suggesting its chaperone activity is crucial for maintaining IMS homeostasis within mitochondria.
Mitochondria, double-membrane organelles, are known to participate in a variety of metabolic and signal transduction pathways. The intermembrane space (IMS) of mitochondria is proposed to subject to multiple damages emanating from the respiratory chain. The optic atrophy 1 (OPA1), an important protein for mitochondrial fusion, is cleaved into soluble short-form (S-OPA1) under stresses. Here we report that S-OPA1 could function as a molecular chaperone in IMS. We purified the S-OPA1 (amino acid sequence after OPA1 isoform 5 S1 site) protein and showed it protected substrate proteins from thermally and chemically induced aggregation and strengthened the thermotolerance of Escherichia coli (E. coli). We also showed that S-OPA1 conferred thermotolerance on IMS proteins, e.g., neurolysin. The chaperone activity of S-OPA1 may be required for maintaining IMS homeostasis in mitochondria.
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