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The sulfhydryl oxidase Erv1 is a substrate of the Mia40-dependent protein translocation pathway |
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| Authors: | Terziyska Nadia Grumbt Barbara Bien Melanie Neupert Walter Herrmann Johannes M Hell Kai |
| Institution: | a Adolf-Butenandt-Institut für Physiologische Chemie, Ludwig-Maximilians-Universität München, Butenandtstrasse 5, D-81377 München, Germany b Cell Biology, University of Kaiserslautern, Erwin-Schrödingerstrasse 13, 67663 Kaiserslautern, Germany |
| Abstract: | The thiol oxidase Erv1 and the redox-regulated receptor Mia40/Tim40 are components of a disulfide relay system which mediates import of proteins into the intermembrane space (IMS) of mitochondria. Here we report that Erv1 requires Mia40 for its import into mitochondria. After passage across the translocase of the mitochondrial outer membrane Erv1 interacts via disulfide bonds with Mia40. Erv1 does not contain twin “CX3C” or twin “CX9C” motifs which are crucial for import of typical substrates of this pathway and it does not need two “CX2C” motifs for import into mitochondria. Thus, Erv1 represents an unusual type of substrate of the Mia40-dependent import pathway. |
| Keywords: | IMS intermembrane space ΔΨ membrane potential FAD flavine adenine dinucleotide NEM N-ethylmaleimide DTT dithiothreitol PK proteinase K |
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