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Ubiquitin-Proteasome Systems Across Domains of Life
Author:        Updatetime:2011-07-18 Printer      Text Size:A A A 

Title: Ubiquitin-Proteasome Systems Across Domains of Life

Presenter: Prof. Julie Maupin-Furlow

University: Department of Microbiology and Cell Science, University of Florida, Gainesville, Florida USA.

Time: 9:30-10:30, 18 July, 2011

Abstract: Proteasomes are amazing nanomachines that catalyze protein degradation and regulate cell function in all eukaryotes, all archaea and in certain bacteria. These enzymatic machines are self-compartmentalized harboring a gated channel which traverses the center of the complex and which includes three chambers. The central most chamber is lined on the interior with 6 to 14 proteolytic active sites. Substrate proteins access these sites with assistance from ATP-dependent regulators that bind, unfold and translocate the proteins into the chambered proteasome. How proteins are marked for proteasome-mediated destruction is more complex than originally imagined with new pathways of ubiquitin-dependent and ubiquitin-independent protein targeting recently discovered. My seminar will focus on the fundamental perspectives of structure and function that are provided by examining proteasomes and ubiquitin-like protein targeting in archaea, one of three domains of life.

Venue: A203, Institute of Microbiology, Chinese Academy of Sciences

 
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