Dr. Yi Shi on structural proteomics of large, native and dynamic assemblies

University of Pittsburgh Department of Biological Sciences Presents:

Dr. Yi Shi
University of Pittsburgh- Department of Cell Biology

"Structural Proteomics of Large, Native and Dynamic Assemblies"

Monday,  April 9, 2018
169 Crawford Hall
11:00 A.M.
10:50 A.M. refreshments

Host: Dr. Karen Arndt  


The yeast nuclear pore complex (NPC) is an organelle-sized macromolecular assembly (> 550 proteins) that pays key roles in the nuclear-cytoplasmic transport of numerous biomolecules. Approximately one-third of NPC proteins contain intrinsically disordered regions which populate the NPC central channel and, through interaction with cargo-carrying transport factors, mediate transport. The sheer size, complexity, and flexibility of the NPC are among the main challenges for a detailed structural characterization of the complex. To overcome these challenges, we have developed novel hybrid approaches that integrate rich and complementary proteomic data including chemical cross-linking/MS that reads residue-specific spatial restraints between and within protein subunits, native and quantitative mass spectrometry for intact mass and protein subunit stoichiometry measurement, cryoEM, and computational modeling that allow us to resolve the complete structure of this organelle-sized protein assembly at unprecedented details {1-3}. We have uncovered a cornucopia of new insights of, e.g., the NPC’s construction principles; how it shapes the nuclear envelope and forms platforms for RNA processing and export {1, 2}; how the central gating machinery is organized and its remarkable “amalgam” evolutionary origin. The new proteomic technologies {1, 3-5} that we have developed for the NPC and other projects will find utilities in solving the structures of large, low-abundance, flexible and dynamic macromolecular assemblies in the cell (5-7).


09 Apr 2018

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