Kai Hell
2025
The Mia40 substrate Mix17 exposes its N-terminus to the cytosolic side of the mitochondrial outer membrane
2025 • Resch Moritz, Johanna Frickel, Korbinian Dischinger, Rachel Choo Shen Wen, Kai Hell, Max Harner
2024
The Mia40 substrate Mix17 exposes its N-terminus to the cytosolic side of the mitochondrial outer membrane
2024 • Resch Moritz, Johanna Frickel, Rachel Choo Shen Wen, Kai Hell, Max Harner, Max E. Harner
2017
A single-cysteine mutant and chimeras of essential Leishmania Erv can complement the loss of Erv1 but not of Mia40 in yeast
2017 • Sandra Specht, Linda Liedgens, Margarida Duarte, Alexandra Stiegler, Ulrike Wirth, Maike Eberhardt, Ana M. Tomás, Kai Hell, Marcel Deponte
2025
Dbi1 is an oxidoreductase and an assembly chaperone for mitochondrial inner membrane proteins
2025 • Soraya Badrie, Kai Hell, Dejana Mokranjac
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Exploring foci of
2025-01-03
Dbi1 is an oxidoreductase and an assembly chaperone for mitochondrial inner membrane proteins
2025-01-03 • Soraya Badrie, Kai Hell, Dejana Mokranjac
Abstract Import and assembly of mitochondrial proteins into multimeric complexes are essential for cellular function. Yet, many steps of these processes and the proteins involved remain unknown. Here, we identify a novel pathway for d isulfide b ond formation and assembly of mitochondrial i nner membrane (IM) proteins. Dbi1, a previously uncharacterized IM protein, interacts with an unassembled pool of Tim17, the central subunit of the presequence translocase of the IM, and is upregulated in cells with increased l…
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Exploring foci of
2025-03-17
The Mia40 substrate Mix17 exposes its N-terminus to the cytosolic side of the mitochondrial outer membrane
2025-03-17 • Resch Moritz, Johanna Frickel, Korbinian Dischinger, Rachel Choo Shen Wen, Kai Hell, Max Harner
ABSTRACT Mitochondrial architecture and the contacts between the mitochondrial outer and the inner membranes depend on the mitochondrial contact site and cristae-organizing system (MICOS) that is highly conserved from yeast to human. Variants in the mammalian MICOS subunit Mic14 (also known as CHCHD10) have been linked to amyotrophic lateral sclerosis and frontotemporal dementia, indicating the importance of this protein. Mic14 has a yeast ortholog, Mix17, a protein of unknown function, which has not been shown to…
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Substrate
Substrate (Chemistry)
N-Terminus
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Exploring foci of
2024-05-31
The Mia40 substrate Mix17 exposes its N-terminus to the cytosolic side of the mitochondrial outer membrane
2024-05-31 • Resch Moritz, Johanna Frickel, Rachel Choo Shen Wen, Kai Hell, Max Harner, Max E. Harner
Abstract Mitochondrial architecture and the contacts between the outer and the inner mitochondrial membrane depend on the mitochondrial contact site and cristae organizing system (MICOS) that is highly conserved from yeast to human. Mutations in the mammalian MICOS subunit Mic14/CHCHD10 have been linked to amyotrophic lateral sclerosis and frontotemporal dementia, indicating the importance of this protein. Mic14/CHCHD10 has a yeast ortholog, Mix17, a protein of unknown function, which has not been shown to interac…
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Substrate
N-Terminus
Substrate (Chemistry)
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Exploring foci of
2017-12-23
A single-cysteine mutant and chimeras of essential Leishmania Erv can complement the loss of Erv1 but not of Mia40 in yeast
2017-12-23 • Sandra Specht, Linda Liedgens, Margarida Duarte, Alexandra Stiegler, Ulrike Wirth, Maike Eberhardt, Ana M. Tomás, Kai Hell, Marcel Deponte
Mia40/CHCHD4 and Erv1/ALR are essential for oxidative protein folding in the mitochondrial intermembrane space of yeast and mammals. In contrast, many protists, including important apicomplexan and kinetoplastid parasites, lack Mia40. Furthermore, the Erv homolog of the model parasite Leishmania tarentolae (LtErv) was shown to be incompatible with Saccharomyces cerevisiae Mia40 (ScMia40). Here we addressed structure-function relationships of ScErv1 and LtErv as well as their compatibility with the oxidative protei…
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