title: Analysis of sDMA modifications of PIWI proteins.
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.
authors.affiliation: Department of Biomedical Sciences, Cedars-Sinai Medical Center, Samuel Oschin Comprehensive Cancer Institute, Los Angeles, CA, USA.
authors.forename: Shozo
authors.initials: S
authors.lastname: Honda
authors.forename: Yoriko
authors.initials: Y
authors.lastname: Kirino
authors.forename: Yohei
authors.initials: Y
authors.lastname: Kirino
mesh_terms: D000595:Amino Acid Sequence; D000818:Animals; D001120:Arginine / Q000031:analogs & derivatives* / Q000378:metabolism; D060565:Argonaute Proteins / Q000737:chemistry* / Q000302:isolation & purification / Q000378:metabolism*; D002460:Cell Line; D004591:Electrophoresis, Polyacrylamide Gel; D047468:Immunoprecipitation; D008297:Male; D051379:Mice; D011499:Protein Processing, Post-Translational; D012261:Ribonucleoproteins / Q000378:metabolism; D016622:Silver Staining; D013737:Testis
chemical_list: D060565:Argonaute Proteins; D012261:Ribonucleoproteins; C487735:dimethylarginine; D001120:Arginine