| ZIM17Gene Symbol: ZIM17 Description: Zim17p Alias: HEP1, TIM15, Zim17p Species: Saccharomyces cerevisiae S288c Sanjuán Szklarz L, Guiard B, Rissler M, Wiedemann N, Kozjak V, van der Laan M, et al. Inactivation of the mitochondrial heat shock protein zim17 leads to aggregation of matrix hsp70s followed by pleiotropic effects on morphology and protein biogenesis. J Mol Biol. 2005;351:206-18 pubmed ..Recent studies led to the identification of Zim17, a mitochondrial zinc finger motif protein that interacts with mtHsp70... Sichting M, Mokranjac D, Azem A, Neupert W, Hell K. Maintenance of structure and function of mitochondrial Hsp70 chaperones requires the chaperone Hep1. EMBO J. 2005;24:1046-56 pubmed ..We report here on a new kind of Hsp70 interacting protein in mitochondria, Hep1. Hep1 is a highly conserved protein present in virtually all eukaryotes... Blamowska M, Sichting M, Mapa K, Mokranjac D, Neupert W, Hell K. ATPase domain and interdomain linker play a key role in aggregation of mitochondrial Hsp70 chaperone Ssc1. J Biol Chem. 2010;285:4423-31 pubmed publisher The co-chaperone Hep1 is required to prevent the aggregation of mitochondrial Hsp70 proteins. We have analyzed the interaction of Hep1 with mitochondrial Hsp70 (Ssc1) and the determinants in Ssc1 that make it prone to aggregation... Díaz de la Loza M, Gallardo M, García Rubio M, Izquierdo A, Herrero E, Aguilera A, et al. Zim17/Tim15 links mitochondrial iron-sulfur cluster biosynthesis to nuclear genome stability. Nucleic Acids Res. 2011;39:6002-15 pubmed publisher ..Cells lacking the mitochondrial chaperone Zim17 (Tim15/Hep1), a component of the iron-sulfur biosynthesis machinery, have limited respiration activity, mimic the .. Burri L, Vascotto K, Fredersdorf S, Tiedt R, Hall M, Lithgow T. Zim17, a novel zinc finger protein essential for protein import into mitochondria. J Biol Chem. 2004;279:50243-9 pubmed ..The central components of the protein import machinery are essential. Here we describe Zim17, an essential protein with a zinc finger motif involved in protein import into mitochondria... Yamamoto H, Momose T, Yatsukawa Y, Ohshima C, Ishikawa D, Sato T, et al. Identification of a novel member of yeast mitochondrial Hsp70-associated motor and chaperone proteins that facilitates protein translocation across the inner membrane. FEBS Lett. 2005;579:507-11 pubmed Here, we report the identification of yeast 15-kD Tim15/Zim17, a new member of mitochondrial Hsp70 (mtHsp70)-associated motor and chaperone (MMC) proteins... Momose T, Ohshima C, Maeda M, Endo T. Structural basis of functional cooperation of Tim15/Zim17 with yeast mitochondrial Hsp70. EMBO Rep. 2007;8:664-70 pubmed Mitochondrial heat-shock protein 70 (mtHsp70) and its partner proteins drive protein import into the matrix. Tim15/Zim17/Hep1 is a mtHsp70 partner protein on the matrix side of the inner mitochondrial membrane... Lewrenz I, Rietzschel N, Guiard B, Lill R, van der Laan M, Voos W. 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. J Biol Chem. 2013;288:30931-43 pubmed publisher 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... Vu M, Zhai P, Lee J, Guerra C, Liu S, Gustin M, et al. The DNLZ/HEP zinc-binding subdomain is critical for regulation of the mitochondrial chaperone HSPA9. Protein Sci. 2012;21:258-67 pubmed publisher ..We also examined if DNLZ is active in vivo. We found that DNLZ partially complements the growth of ?zim17 Saccharomyces cerevisiae, and we discovered that a Zim17 truncation lacking a majority of the C-terminal subdomain ..
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