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Proteomics01:33

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.
Proteomics is the study of proteomes' function. It involves the large-scale systematic study of the proteome to denote the protein complement expressed by a genome. Scientist Mark Wilkins coined the term...
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Chemical proteomic approaches to investigate N-myristoylation.

James Zhang1, Wouter W Kallemeijn2, Sarah Hassan3

  • 1Department of Chemistry, Imperial College London, London, United Kingdom; The Francis Crick Institute, London, United Kingdom; Division of Clinical Studies, The Institute of Cancer Research (ICR) & Royal Marsden NHS Trust, London, United Kingdom.

Methods in Enzymology
|August 31, 2025
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Summary

This study details two chemical proteomic methods to analyze N-myristoylation, a crucial protein lipidation process. These techniques enable researchers to study N-myristoylation in various biological contexts and in response to drug treatments.

Keywords:
ChemoproteomicsLipidationMetabolic labellingN-myristoylationNMTSortase AYnMyr

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Area of Science:

  • Biochemistry
  • Proteomics
  • Chemical Biology

Background:

  • N-myristoylation is a key protein lipidation catalyzed by N-myristoyltransferase (NMT) enzymes, affecting over 200 proteins with N-terminal glycines.
  • This modification regulates protein localization, stability, function, and interactions, playing a role in biological processes and diseases.
  • Understanding N-myristoylation changes in disease and during NMT inhibition is vital for basic biology and clinical applications.

Purpose of the Study:

  • To describe two complementary chemical proteomic methods for assessing N-myristoylation.
  • To provide detailed protocols for these methods, aiding research into N-myristoylation's role in biology and disease.

Main Methods:

  • Metabolic labeling: Incorporating bio-orthogonal myristic acid analogs into NMT substrates for selective labeling, enrichment, and detection.
  • Sortase A-mediated labeling: Using Sortase A to attach an enrichment handle to NMT substrates, particularly useful when NMT activity is inhibited.

Main Results:

  • The chapter presents detailed protocols for both metabolic labeling and Sortase A-based chemical proteomic approaches.
  • These methods allow for the selective labeling, enrichment, and detection of N-myristoylated proteins.
  • The protocols cover cell treatment, sample preparation, and data analysis for comprehensive N-myristoylation profiling.

Conclusions:

  • Two robust chemical proteomic methods are presented for profiling the N-myristoylated proteome.
  • These techniques are valuable for investigating N-myristoylation in health, disease, and response to NMT inhibitors.
  • The provided protocols facilitate advancements in understanding N-myristoylation's biological roles and therapeutic potential.