STRUCTURAL STUDIES OF THE MOLECULAR CHAPERONES-HSP104/CLPB

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This subproject is one of many research subprojects utilizing the resources provided by a Center grant funded by NIH/NCRR. The subproject and investigator (PI) may have received primary funding from another NIH source, and thus could be represented in other CRISP entries. The institution listed is for the Center, which is not necessarily the institution for the investigator. ClpB/Hsp104 are ATP-dependent molecular chaperones and form hexameric, single ring structures of 600 kDa. We have solved the crystal structure of ClpB full-length bound to AMPPNP (Lee et al., 2003)To address the structural basis of substrate recognition, we have now crystallized a full-lenth ClpB-peptide complex and wish to determine the structure of this complex using x-ray crystallography. In addition to its role in thermotolerance, Hsp104 is also required for the inheritance and maintenance of [PSI+], a yeast prion-like element that, similar to its mammalian counterpart, is characterized by amyloid fiber formation. We wish to determine the crystal structure of Hsp104 to study the structure and function of Hsp104 in [PSI+] propagation.