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Investigating the roles of ribosome-associated proteins in translational regulation of gene expression

Abstract

The ribosome has long been regarded as the protein producing center of the cell, yet we are still defining its role as a target of gene regulation in the cell. Towards this end, I developed a proteomics-based approach to uncover novel ribosome-associated proteins that regulate translation in the cell. I also worked with the Kopito Lab at Stanford University to understand why a core ribosomal protein, RPL26, is post-translationally modified by a ubiquitin-like protein, UFM1. Additionally, I collaborated with the Corn Lab at UC Berkeley and ETH Zurich to describe how double-stranded DNA damage leads to the depletion of core ribosomal proteins, RPL40 and RPS27A. These projects demonstrate that ribosome composition is neither static nor homogeneous but can be altered depending on the environmental and cellular context.

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