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Updated: Dec 20, 2025

Phosphoproteomic Strategy for Profiling Osmotic Stress Signaling in Arabidopsis
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Label-Free Quantitative Phosphoproteomics for Algae.

Megan M Ford1, Sheldon R Lawrence1, Emily G Werth1

  • 1Department of Chemistry, University of North Carolina at Chapel Hill, Chapel Hill, NC, USA.

Methods in Molecular Biology (Clifton, N.J.)
|May 29, 2020
PubMed
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Researchers developed a reproducible method using TiO2-based phosphopeptide enrichment and label-free LC-MS/MS to quantify phosphorylation in Chlamydomonas reinhardtii. This approach enhances the study of posttranslational modifications in photosynthetic organisms.

Area of Science:

  • * Molecular Biology
  • * Biochemistry
  • * Photosynthetic Organism Research

Background:

  • * Chlamydomonas reinhardtii is a key model organism for studying microalgal processes, including metabolic signaling and phosphorylation networks.
  • * Proteomic analysis, particularly mass spectrometry-based methods, is crucial for understanding posttranslational modifications (PTMs) like phosphorylation.
  • * Accurate quantification of dynamic PTMs, such as phosphorylation, is challenging due to substoichiometric levels and requires high sensitivity and reproducibility.

Purpose of the Study:

  • * To present a novel method for high-throughput phosphoproteome quantification in Chlamydomonas reinhardtii.
  • * To improve the reproducibility and sensitivity of analyzing phosphorylation events.
  • * To establish a widely applicable approach for studying phosphorylation in photosynthetic organisms.
Keywords:
AlgaeChlamydomonas reinhardtiiLabel-freeMass spectrometryPhosphorylationQuantitative proteomics

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Last Updated: Dec 20, 2025

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Main Methods:

  • * Utilized titanium dioxide (TiO2)-based phosphopeptide enrichment.
  • * Employed label-free liquid chromatography-tandem mass spectrometry (LC-MS/MS).
  • * Processed three technical replicate samples of Chlamydomonas.

Main Results:

  • * Quantified a total of 1775 phosphoproteins and 3595 phosphosites.
  • * Achieved a median coefficient of variation (CV) of 21% for quantified phosphopeptides.
  • * Demonstrated high reproducibility for analyzing phosphorylation events in differential studies.

Conclusions:

  • * The developed TiO2-based enrichment and label-free LC-MS/MS method provides a reproducible approach for phosphoproteome quantification.
  • * This method facilitates in-depth analysis of phosphorylation in Chlamydomonas and other photosynthetic organisms.
  • * The approach is adaptable for broader applications in studying dynamic posttranslational modifications.