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The Role of the Eukaryotic Elongation Factor 1Bgamma in Protein Trafficking and the Oxidative Stress Response

Anthony Michael Esposito
Bachelor of Science, 2004
City University of New York
College of Staten Island

Graduate Program: Molecular Genetics, Microbiology and Immunology

Thesis Advisor: Terri Goss Kinzy, PhD

RWJMS Research Tower
Room 747

Wednesday, April 21, 2010
10:00 am


The turnover of damaged proteins is critical to cell survival during stressful conditions such as heat shock or oxidative stress. The accumulation of misfolded proteins in the cytoplasm or ER is toxic to cells and must therefore be efficiently exported from the ER and recycled by the proteasome or the vacuole. Previously it was shown that the loss of eukaryotic elongation factor 1Bgamma (eEF1Bgamma) from the yeast Saccharomyces cerevisiae results in resistance to oxidative stress. Strains lacking the eEF1Bgamma show severe defects in protein turnover during conditions of oxidative stress. Furthermore, they accumulate a greater amount of oxidized proteins resulting in an increase in heat shock chaperone levels. These strains show severe defects in vacuole morphology and defects related to the ER-Golgi transport of carboxypeptidase Y (CPY) that is not dependent on the catalytic function of the eEF1B complex as a guanine nucleotide exchange factor. Finally, eEF1Bgamma was shown to co-immunoprecipitate with an essential component of ER-Golgi transport vesicles. Taken together these results support a role for eEF1Bgamma in ER-Golgi transport.

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