Structur and function of mutants of the 20S proteasome from S. cerevisiae (Struktur und Funktion von Mutanten des 20S Proteasoms aus S. cerevisiae)

• Applicant: Professor Dr. Robert Huber
• Subject Area: Biochemistry
• Term: from 1998 to 2003
• Project identifier: Deutsche Forschungsgemeinschaft (DFG) - Project number 5112948

Based on the crystal structure of the 20S proteasome from yeast, determined in 1997, we want to investigate structure and function of mutants and peptide complexes, with special emphasis on those, that influence substrate access to the proteolytic chamber. We would like to determine the role of proteasome associated proteins looking at the structure of either isolated components or protein complexes. In particular, we want to focus on the ATPase subunits of the yeast and archaebacterial proteasomes. The eubacterial proteasome analogue Hs1VU will also be analysed structurally.

• DFG Programme: Priority Programmes
• Subproject of: SPP 1045: Struktur, Funktion und Regulation des 20S/26S Ubiquitin-Proteasomsystems