Background

Covalent protein modifications play key roles in modulating protein function, stability, localization, and interactions. During protein synthesis, some protein modifications have been described, for example acetylation. However, how protein modifications affect co-translational protein folding and homeostasis is an underexplored but an important question in biology. 

Project

Our joint project will characterize the function of co-translational protein modifications (CTMs) on the nascent proteome. We will integrate ribosome profiling (Frydman lab at Stanford), large-scale CRISPR-Cas9 mutagenesis (Steinmetz lab at EMBL), and proteomics (Savitski lab at EMBL) to identify sites of CTMs of nascent chains, and define their function in reshaping and regulating the nascent proteome. This work will establish a new conceptual paradigm on co-translational proteostasis that could be extended to additional modes of co-translational covalent regulation of protein biogenesis. Our work will uncover an underexplored aspect of co-translational proteostasis that may have important implications for pathologies associated to the dysregulation of protein modification and proteostasis, such as aging and neurodegenerative diseases.

This project is supported by a Bridging Excellence Fellowship awarded to Maximilian Seidel

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