Global Analysis of Protein Arginylation
Author Information
Author(s): Catherine C. L. Wong, Tao Xu, Reena Rai, Aaron O. Bailey, John R. Yates III, Yuri I. Wolf, Henry Zebroski, Anna Kashina
Primary Institution: The Scripps Research Institute
Hypothesis
What are the molecular effects and identities of proteins arginylated in vivo?
Conclusion
Protein arginylation is a general mechanism for regulating protein structure and function, affecting various physiological systems.
Supporting Evidence
- The study identified 43 proteins that are arginylated in vivo.
- Arginylation can occur on various N-terminally exposed residues, not just Asp, Glu, or Cys.
- The identified proteins are involved in cytoskeletal and metabolic pathways.
Takeaway
This study found that proteins can be modified by adding arginine, which helps control how they work in the body, especially during development.
Methodology
The study used a knockout mouse model and techniques like 2D gel electrophoresis, metabolic labeling, and mass spectrometry to identify arginylated proteins.
Limitations
The study may not account for all arginylated proteins, especially those that are metabolically destabilized.
Digital Object Identifier (DOI)
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