Article
The functional interaction of mitochondrial Hsp70s with the escort protein Zim17 is critical for Fe/S biogenesis and substrate interaction at the inner membrane preprotein translocase.
The Journal of biological chemistry - 25 Oct 2013
Lewrenz Ilka, Rietzschel Nicole, Guiard Bernard, Lill Roland, van der Laan Martin, Voos Wolfgang
Abstract excerpt
The yeast protein Zim17 belongs to a unique class of co-chaperones that maintain the solubility of Hsp70 proteins in mitochondria and plastids of eukaryotic cells. However, little is known about the functional cooperation between Zim17 and mitochondrial Hsp70 proteins in vivo. To analyze the effects of a loss of Zim17 function in the authentic environment, we introduced novel conditional mutations within the...
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