A disulfide bond in the TIM23 complex is crucial for voltage gating and mitochondrial protein import
Abstract: Tim17 is a central, membrane-embedded subunit of the mitochondrial protein import machinery. In this study, we show that Tim17 contains a pair of highly conserved cysteine residues that form a structural disulfide bond exposed to the intermembrane space (IMS). This disulfide bond is critical for efficient protein translocation through the TIM23 complex and for dynamic gating of its preprotein-conducting channel. The disulfide bond in Tim17 is formed during insertion of the protein into the inner membrane. Whereas the import of Tim17 depends on the binding to the IMS protein Mia40, the oxidoreductase activity of Mia40 is surprisingly dispensable for Tim17 oxidation. Our observations suggest that Tim17 can be directly oxidized by the sulfhydryl oxidase Erv1. Thus, import and oxidation of Tim17 are mediated by the mitochondrial disulfide relay, though the mechanism by which the disulfide bond in Tim17 is formed differs considerably from that of soluble IMS proteins
- Location
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Deutsche Nationalbibliothek Frankfurt am Main
- Extent
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Online-Ressource
- Language
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Englisch
- Notes
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The journal of cell biology. - 214, 4 (2016) , 417-431, ISSN: 1540-8140
- Event
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Veröffentlichung
- (where)
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Freiburg
- (who)
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Universität
- (when)
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2025
- Creator
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Ramesh, Ajay
Peleh, Valentina
Martinez-Caballero, Sonia
Wollweber, Florian
Sommer, Frederik
Laan, Martin van der
Schroda, Michael
Alexander, R. Todd
Campo, María Luisa
Herrmann, Johannes
- DOI
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10.1083/jcb.201602074
- URN
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urn:nbn:de:bsz:25-freidok-1364858
- Rights
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Open Access; Der Zugriff auf das Objekt ist unbeschränkt möglich.
- Last update
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15.08.2025, 7:30 AM CEST
Data provider
Deutsche Nationalbibliothek. If you have any questions about the object, please contact the data provider.
Associated
- Ramesh, Ajay
- Peleh, Valentina
- Martinez-Caballero, Sonia
- Wollweber, Florian
- Sommer, Frederik
- Laan, Martin van der
- Schroda, Michael
- Alexander, R. Todd
- Campo, María Luisa
- Herrmann, Johannes
- Universität
Time of origin
- 2025
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A structural disulfide bond ín the mitochondrial ΤΙΜ23 translocase is critical for voltage gating and efficient protein import
Voltage gating of mechanosensitive PIEZO channels
Mechanochemistry of disulfide bonds in proteins
Mechanochemistry of Disulfide Bonds in Proteins
Voltage-gating and assembly of split Kv10.1 channels
Structural determinants of voltage-dependent gating of Kv10.1
Protein crystal quality oriented disulfide bond engineering
Rhodium-Catalyzed Formation of Disulfide Bonds in Water
Electrochemical gating of oxide nanowire transistors of low operating voltage
Electrochemical Gating of Oxide Nanowire Transistors at Low Operating Voltage
Voltage-dependent gating of SV channel TPC1 confers vacuole excitability
Structure, gating and interactions of the voltage-dependent anion channel
A structural disulfide bond ín the mitochondrial ΤΙΜ23 translocase is critical for voltage gating and efficient protein import
Voltage gating of mechanosensitive PIEZO channels
Mechanochemistry of disulfide bonds in proteins
Mechanochemistry of Disulfide Bonds in Proteins
Voltage-gating and assembly of split Kv10.1 channels
Structural determinants of voltage-dependent gating of Kv10.1
Protein crystal quality oriented disulfide bond engineering
Rhodium-Catalyzed Formation of Disulfide Bonds in Water
Electrochemical gating of oxide nanowire transistors of low operating voltage
Electrochemical Gating of Oxide Nanowire Transistors at Low Operating Voltage
Voltage-dependent gating of SV channel TPC1 confers vacuole excitability