ArticleScientific reports2016
The presence of disulfide bonds reveals an evolutionarily conserved mechanism involved in mitochondrial protein translocase assembly.
Article in Scientific reports, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.
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Who cites it
23 citing papers in PubMed, 47 citations in OpenAlex.
- Redox signals and oxidative stress in the control of mitochondrial protein import.Protein science : a publication of the Protein Society · 2026Review
- Molecular machineries and pathways of mitochondrial protein transport.Nature reviews. Molecular cell biology · 2025Review
- Active control of mitochondrial network morphology by metabolism-driven redox state.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- Article
- Structure prediction analysis of human core TIM23 complex reveals conservation of the protein translocation mechanism.FEBS open bio · 2024Article
- Two domains of Tim50 coordinate translocation of proteins across the two mitochondrial membranes.Life science alliance · 2023Article
- Article
- CHCHD4 (MIA40) and the mitochondrial disulfide relay system.Biochemical Society transactions · 2021Review
- Targeting and Insertion of Membrane Proteins in Mitochondria.Frontiers in cell and developmental biology · 2021Review
- Role of the Mitochondrial Protein Import Machinery and Protein Processing in Heart Disease.Frontiers in cardiovascular medicine · 2021Review
- Tim17 Updates: A Comprehensive Review of an Ancient Mitochondrial Protein Translocator.Biomolecules · 2020Review
- Cysteine residues in mitochondrial intermembrane space proteins: more than just import.British journal of pharmacology · 2019Review
- Mutations of the mitochondrial carrier translocase channel subunit TIM22 cause early-onset mitochondrial myopathy.Human molecular genetics · 2018Article
- A new mitofusin topology places the redox-regulated C terminus in the mitochondrial intermembrane space.The Journal of cell biology · 2018Article
- Hsp70 at the membrane: driving protein translocation.BMC biology · 2018Review
- The divergent N-terminal domain of Tim17 is critical for its assembly in the TIM complex in Trypanosoma brucei.Molecular and biochemical parasitology · 2017Article
- Protein trafficking in the mitochondrial intermembrane space: mechanisms and links to human disease.The Biochemical journal · 2017Review
- Role of Tim17 Transmembrane Regions in Regulating the Architecture of Presequence Translocase and Mitochondrial DNA Stability.Molecular and cellular biology · 2017Article
- Article
- TIM29 is a subunit of the human carrier translocase required for protein transport.FEBS letters · 2016Article
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Authors and funding
4 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Disulfide bond formation is crucial for the biogenesis and structure of many proteins that are localized in the intermembrane space of mitochondria. The importance of disulfide bond formation within mitochondrial proteins was extended beyond soluble intermembrane space proteins. Tim22, a membrane protein and core component of the mitochondrial translocase TIM22, forms an intramolecular disulfide bond in yeast. Tim22 belongs to the Tim17/Tim22/Tim23 family of protein translocases. Here, we present evidence of the high evolutionary conservation of disulfide bond formation in Tim17 and Tim22 among fungi and metazoa. Topological models are proposed that include the location of disulfide bonds relative to the predicted transmembrane regions. Yeast and human Tim22 variants that are not oxidized do not properly integrate into the membrane complex. Moreover, the lack of Tim17 oxidation disrupts the TIM23 translocase complex. This underlines the importance of disulfide bond formation for mature translocase assembly through membrane stabilization of weak transmembrane domains.
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