1 ATPase domain and interdomain linker play a key role in aggregation of mitochondrial Hsp 70 chaperone Ssc 1

@inproceedings{Blamowska20091AD,
  title={1 ATPase domain and interdomain linker play a key role in aggregation of mitochondrial Hsp 70 chaperone Ssc 1},
  author={Marta Blamowska and Martin Sichting and Koyeli Mapa and Dejana Mokranjac and Walter Neupert},
  year={2009}
}
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 which make it prone to aggregation. The ATPase and the peptide binding domain (PBD) of Hsp70 proteins are connected by a linker segment that mediates interdomain communication between the domains. We show here that the minimal Hep1 binding entity of Ssc1 consists of the ATPase domain and the… CONTINUE READING

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