Details

Autor(en) / Beteiligte

• Mesecke, Nikola
• Bihlmaier, Karl
• Grumbt, Barbara
• Longen, Sebastian
• Terziyska, Nadia
• Hell, Kai
• Herrmann, Johannes M

Titel

The zinc-binding protein Hot13 promotes oxidation of the mitochondrial import receptor Mia40

Ist Teil von

• EMBO reports, 2008-11, Vol.9 (11), p.1107-1113

Ort / Verlag

Chichester, UK: John Wiley & Sons, Ltd

Erscheinungsjahr

2008

Link zum Volltext

Quelle

MEDLINE

Beschreibungen/Notizen

• A disulphide relay system mediates the import of cysteine‐containing proteins into the intermembrane space of mitochondria. This system consists of two essential proteins, Mia40 and Erv1, which bind to newly imported proteins by disulphide transfer. A third component, Hot13, was proposed to be important in the biogenesis of cysteine‐rich proteins of the intermembrane space, but the molecular function of Hot13 remained unclear. Here, we show that Hot13, a conserved zinc‐binding protein, interacts functionally and physically with the import receptor Mia40. It improves the Erv1‐dependent oxidation of Mia40 both in vivo and in vitro. As a consequence, in mutants lacking Hot13, the import of substrates of Mia40 is impaired, particularly in the presence of zinc ions. In mitochondria as well as in vitro, Hot13 can be functionally replaced by zinc‐binding chelators. We propose that Hot13 maintains Mia40 in a zinc‐free state, thereby facilitating its efficient oxidation by Erv1.