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In Vivo Proximity Biotinylation for Protein Interaction Studies in Paramecium tetraurelia
Published on: September 12, 2025
Analysis of sDMA modifications of PIWI proteins
Shozo Honda1, Yoriko Kirino, Yohei Kirino
1Department of Biomedical Sciences, Cedars-Sinai Medical Center, Samuel Oschin Comprehensive Cancer Institute, Los Angeles, CA, USA.
Abstract:
Arginine methylation is an important posttranslational protein modification that modulates protein function for a wide range of biological processes. PIWI proteins, a subclade of the Argonaute family proteins, contain evolutionarily conserved symmetrical dimethylarginines (sDMAs). It has become increasingly apparent that the sDMAs of PIWI proteins serve as binding elements for TUDOR domain-containing proteins and that sDMA-dependent protein interactions play crucial roles in the biogenesis and function of PIWI-interacting RNAs (piRNAs). We describe a method for detecting PIWI sDMAs and purifying PIWI/piRNA complexes using anti-sDMA antibodies.
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