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Please use this identifier to cite or link to this item: http://hdl.handle.net/1807/25704

Title: The Small Ubiquitin-related Mmodifier in the Stress Response and the Use of Mass Spectrometry/SUMmOn for Identification of Ubiquitin and Ubiquitin-like Protein Conjugation Sites
Authors: Jeram, Stanley Martin
Advisor: Raught, Brian
Department: Medical Biophysics
Keywords: SUMO
mass spectrometry
ubiquitin
alcohol stress
NEDD8
SUMmOn
Issue Date: 3-Jan-2011
Abstract: Ubiquitin (Ub) and the ubiquitin-like proteins (Ubls) are polypeptides that can be covalently conjugated to a variety of “target” molecules to modulate their turnover rate, localization and/or function. The full range of Ubl functions is only beginning to be understood. The Raught lab is using mass spectrometry and high throughput screening methods, along with standard cell biology and biochemistry approaches, to better understand Ubl function. Here, I describe the role of a Ubl called small ubiquitin-related modifier (SUMO) in the budding yeast alcohol stress response. We identified a regulatory mechanism of the SUMO system, involving modulation of the localization of a SUMO protease. Secondly, using mass spectrometry (MS), I assisted in identifying several yeast and mammalian Ubl “chain” linkages. Finally, I propose an integrated MS methodology designed to complement standard database software for the confident identification of Ub/Ubl conjugation sites.
URI: http://hdl.handle.net/1807/25704
Appears in Collections:Master

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