Yonghao Yu
Department of Chemistry
Genome Center
University of California
Davis, CA 95616
(530) 754-4038
yyh@berkeley.edu
Position:Graduate Student Researcher
Education:B.S. in Chemistry, Fudan University, China, 1997-2001
Research Topic:characterization of protein-ligand noncovalent complex using FT-ICR mass spectrometry
Research Summary:Many viruses use a highly structured RNA sequence, internal ribosome entry site (IRES), to initiate protein synthesis. We are interested in a comprehensive mapping of the all the proteins and the associated protein factors of the IRES bound 40S ribosome using both of the top-down and bottom-up mass spectrometry approaches, which will facilitate the understanding of the IRES-ribosome recruitment mechanism. After fractionation of native 40S ribosome subunits by reverse phase HPLC, human 40S ribosomal proteins (XX phenotype) were identified using the top down approach. All of the 40S ribosomal proteins identified by the top down approach were found to contain various posttranslational modifications, including loss of methionine, N-terminal acetylation, methylation and disulfide bonds. Using the bottom-up approach, we identified all but one 40S ribosomal proteins. For the IRES pull-down 40S ribosome subunit, nucleolin and various eIF3 subunits were found, which were not present in native 40S subunit and thus may be involved in IRES mediated translation. Experiments are ongoing to identify various post-translational modifications.

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