Oral presentationIdentification and characterisation of Hsp70-containing protein complexes from Saccharomyces cerevisiaePC Van Breugel† , CPAM Kolen, H van Heerikhuizen and SM van der Vies Department of Biochemistry and Molecular Biology, Vrije Universiteit Amsterdam, De Boelelaan 1083, 1081 HV Amsterdam, The Netherlands † Presenting author Meeting of the Benelux Yeast Research Groups Leuven, Belgium, 4 May 2001 Yeasterday 2001,
1:or010
| Received: |
5 June 2001 |
| Published: |
5 June 2001 |
Oral presentation
The Hsp70 family comprises an abundant and highly conserved group of molecular chaperones and are found in prokaryotes and most sub-cellular compartments of the eukaryotic cell. Members of this family are involved in a variety of cellular processes including polypeptide folding, translocation, activation and degradation. Hsp70 functions through cycles of binding and release of substrate proteins, co-chaperones and ATP/ADP. Examples of co-chaperones are Hsp40, which stimulates the ATPase activity of Hsp70 and the Hsp70-interacting protein (Hip), which stabilises the binding of ADP. We use the yeast S. cerevisiae for further exploration of Hsp70 and with a focus on the cytosolic Ssa1-4 subfamily. To obtain information regarding the function of Ssa proteins we have started to isolate and characterise Ssa4p-containing complexes using either native PAGE or co-immunoprecipitation in combination with Mass Spectrometry (MALD-MS). This approach has lead to the identification of Ssa4p-containing complexes. One of the proteins in these complexes turned out to be Sse1p, a member of the Hsp110 group of molecular chaperones. Interestingly the interaction between Ssa4p and Sse1p is disrupted in the presence of Mg-ATP.
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