期刊
CELL REPORTS
卷 18, 期 11, 页码 2729-2741出版社
CELL PRESS
DOI: 10.1016/j.celrep.2017.02.053
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资金
- BBSRC
- Wellcome Trust
- University of Manchester Strategic Fund
- Wellcome Trust PhD studentship [096604/Z/11/Z]
- BBSRC project grant [BB/M020770/1]
- Wellcome Trust Institutional Strategic Support Funds to the University of Glasgow [097821/Z11/Z]
- Scottish Universities Life Science Alliance
- Scottish Funding Council [HR07019]
- Royal Society-Wolfson research merit award [WM120111]
- BBSRC [BB/M020770/1] Funding Source: UKRI
- Wellcome Trust [096604/Z/11/Z] Funding Source: Wellcome Trust
- Biotechnology and Biological Sciences Research Council [BB/M020770/1] Funding Source: researchfish
Thiol peroxidases are conserved hydrogen peroxide scavenging and signaling molecules that contain redox-active cysteine residues. We show here that Gpx3, the major H2O2 sensor in yeast, is present in the mitochondrial intermembrane space (IMS), where it serves a compartment-specific role in oxidative metabolism. The IMS-localized Gpx3 contains an 18-amino acid N-terminally extended form encoded from a non-AUG codon. This acts as a mitochondrial targeting signal in a pathway independent of the hitherto known IMS-import pathways. Mitochondrial Gpx3 interacts with the Mia40 oxidoreductase in a redox-dependent manner and promotes efficient Mia40-dependent oxidative protein folding. We show that cells lacking Gpx3 have aberrant mitochondrial morphology, defective protein import capacity, and lower inner membrane potential, all of which can be rescued by expression of a mitochondrial- only form of Gpx3. Together, our data reveal a novel role for Gpx3 in mitochondrial redox regulation and protein homeostasis.
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