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Proteomics

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A proteome is the entire set of proteins that a cell type produces. We can study proteomes using the knowledge of genomes because genes code for mRNAs, and the mRNAs encode proteins. Although mRNA analysis is a step in the right direction, not all mRNAs are translated into proteins.
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Updated: Jun 19, 2026

Detection of Protein Ubiquitination Sites by Peptide Enrichment and Mass Spectrometry

Detection of Protein Ubiquitination Sites by Peptide Enrichment and Mass Spectrometry

Published on: March 23, 2020

An Unbiased Proteomic Platform for ATE1-based Arginylation Profiling.

Zongtao Lin¹, Yixuan Xie¹, Joanna Gongora¹

¹Department of Biochemistry and Molecular Biophysics, Washington University in St. Louis, St. Louis, MO 63110.

Biorxiv : the Preprint Server for Biology

|June 10, 2024

Summary

This summary is machine-generated.

Protein arginylation, a crucial modification catalyzed by ATE1, is now identifiable using our novel activity-based arginylation profiling (ABAP) platform. This method accurately distinguishes arginylation from translation, revealing new modification sites.

Keywords:

arginylation arginyltransferase posttranslational modification protein profiling proteomics

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Area of Science:

Biochemistry
Proteomics
Post-translational Modifications

Background:

Protein arginylation is a vital post-translational modification (PTM) catalyzed by arginyl-tRNA-protein transferase 1 (ATE1).
Differentiating arginylation from translational arginine residues is challenging due to identical mass.
Existing methods lack the specificity to unbiasedly identify arginylation substrates and sites.

Purpose of the Study:

To develop a general activity-based arginylation profiling (ABAP) platform.
To enable unbiased discovery of arginylation substrates and precise modification sites.
To overcome the challenge of distinguishing arginylation from translational arginine residues.

Main Methods:

Integration of isotopic arginine labeling into an ATE1 assay using biological lysates (ex vivo).
Elimination of translational bias by avoiding live cells and ribosomal activity.
Application of the ABAP platform to diverse sample types including peptides, proteins, cells, and tissues.

Main Results:

Successfully identified 229 unique arginylation sites in human proteomes.
Demonstrated the platform's applicability across various sample types with minimal input (20 μg).
Validated representative arginylation sites and initiated functional follow-up studies.

Conclusions:

The ABAP platform provides a robust method for bona fide arginylation identification.
This technology facilitates the functional characterization of arginylation.
The platform is globally applicable, paving the way for broader research into protein arginylation.