Structure and Function Analysis of the Protein Degradation Machinery

Dr. Michal Sharon Incumbent of the Elaine Blond Career Development Chair Office: Ullman Building, Room 223 Tel: +972-8-934-3947 Fax: +972-8-934-6010 E-mail: michal.sharon@weizmann.ac.il CV

Our group is interested in the relationship between structure and function of the proteasome complex and other molecular machines involved in the ubiquitin-proteasome pathway.

Our objective is to understand how these macromolecular complexes are arranged, assemble and function. We study the mechanisms that control and regulate these cellular machines and explore the network of intermolecular interactions that ensure the integration of cellular processes.

We apply a novel structural mass spectrometry approach that allows to maintain large cellular complexes intact in the gas phase. The fundamental advantage of this approach lies in its ability to probe transient, asymmetric and heterogeneous macromolecular complexes, using very low concentration of sample.

The protein degradation machinery: In the ubiquitin-proteasome pathway, energy from ATP is used to tag an unwanted protein with a chain of ubiquitins marking it for destruction. The protein is then hydrolyzed into small peptide fragments by the proteasome.