title: Arginine methylation of the cellular nucleic acid binding protein does not affect its subcellular localization but impedes RNA binding.
abstract: Cellular nucleic acid binding protein (CNBP) contains seven zinc finger (ZF) repeats and an arginine and glycine (RG) rich sequence between the first and the second ZF. CNBP interacts with protein arginine methyltransferase PRMT1. Full-length but not RG-deleted or mutated CNBP can be methylated. Treatment with a methylation inhibitor AdOx reduced CNBP methylation, but did not affect the concentrated nuclear localization of CNBP. Nevertheless, arginine methylation of CNBP appeared to interfere with its RNA binding activity. Our findings show that arginine methylation of CNBP in the RG motif did not change the subcellular localization, but regulated its RNA binding activity.
authors.affiliation: Department of Biomedical Sciences, Chung Shan Medical University, Taichung, Taiwan, ROC.
authors.forename: Hung-Ming
authors.initials: HM
authors.lastname: Wei
authors.affiliation: Department of Biomedical Sciences, Chung Shan Medical University, Taichung, Taiwan, ROC.
authors.forename: Huan-Hsuan
authors.initials: HH
authors.lastname: Hu
authors.affiliation: Department of Biomedical Sciences, Chung Shan Medical University, Taichung, Taiwan, ROC.
authors.forename: Gia-Yun
authors.initials: GY
authors.lastname: Chang
authors.affiliation: Institute of Biochemistry and Biotechnology, Chung Shan Medical University, Taichung, Taiwan, ROC.
authors.forename: Yu-Jen
authors.initials: YJ
authors.lastname: Lee
authors.affiliation: Department of Biomedical Sciences, Chung Shan Medical University, Taichung, Taiwan, ROC.
authors.forename: Yi-Chen
authors.initials: YC
authors.lastname: Li
authors.affiliation: Institute of Oral Biology, Chung Shan Medical University, Taichung, Taiwan, ROC.
authors.forename: Hong-How
authors.initials: HH
authors.lastname: Chang
authors.affiliation: Department of Biomedical Sciences, Chung Shan Medical University, Taichung, Taiwan, ROC; Department of Medical Research, Chung Shan Medical University Hospital, Taichung, Taiwan, ROC. Electronic address: cli@csmu.edu.tw.
authors.forename: Chuan
authors.initials: C
authors.lastname: Li
mesh_terms: D020816:Amino Acid Motifs; D001120:Arginine / Q000737:chemistry / Q000378:metabolism*; D001667:Binding, Competitive; D006367:HeLa Cells; D006801:Humans; D008745:Methylation; D011485:Protein Binding; D011499:Protein Processing, Post-Translational; D021381:Protein Transport; D011484:Protein-Arginine N-Methyltransferases / Q000378:metabolism; D012313:RNA / Q000737:chemistry; D016601:RNA-Binding Proteins / Q000737:chemistry / Q000378:metabolism*; D012097:Repressor Proteins / Q000378:metabolism
chemical_list: C433227:CNBP protein, human; D016601:RNA-Binding Proteins; D012097:Repressor Proteins; D012313:RNA; D001120:Arginine; C099988:PRMT1 protein, human; D011484:Protein-Arginine N-Methyltransferases
keywords: CNBP; Protein arginine methylation; RNA binding