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A Large-Scale Method to Measure the Stoichiometries of Protein Poly-ADP-Ribosylation
Peng Li1, Yajie Zhang1, Chiho Kim2
1Department of Biochemistry, University of Texas Southwestern Medical Center, Dallas, Texas 75390, United States.
ACS Chemical Biology
|February 26, 2026
Summary
Researchers quantified protein poly-ADP-ribosylation (PARylation) stoichiometries in eukaryotes. High PARylation levels (>1%) mainly affect transcription and chromatin remodeling proteins, offering insights into protein function.
Area of Science:
- Biochemistry
- Molecular Biology
- Genetics
Background:
- Poly-ADP-ribosylation (PARylation) is a crucial post-translational modification in eukaryotes.
- The biological roles of most PARylated proteins are not well understood.
- PARylation stoichiometry is key to determining protein function.
Purpose of the Study:
- To develop a large-scale method for measuring protein PARylation stoichiometries.
- To quantify PARylation levels across a broad range of proteins.
- To identify proteins with high PARylation occupancy.
Main Methods:
- Chemically mild cell lysis
- Boronate affinity enrichment
- Titration experiments
- Analysis of 235 proteins
Main Results:
- Developed a method to measure PARylation stoichiometries for 235 proteins.
- Demonstrated PARylation occupancy spans over 3 orders of magnitude.
- Found most PARylation events occur at low stoichiometry (median 0.58%).
- Identified high-stoichiometry PARylation (>1%) in transcription and chromatin remodeling proteins.
Conclusions:
- This study provides a quantitative, system-wide view of PARylation stoichiometries.
- The findings offer a valuable resource for future functional studies of PARylation.
- High PARylation specifically targets key regulatory proteins involved in transcription and chromatin remodeling.
