Arginine methylation of the cellular nucleic acid binding protein does not affect its subcellular localization but impedes RNA binding |
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| Affiliation: | 1. Department of Biomedical Sciences, Chung Shan Medical University, Taichung, Taiwan, ROC;2. Institute of Biochemistry and Biotechnology, Chung Shan Medical University, Taichung, Taiwan, ROC;3. Institute of Oral Biology, Chung Shan Medical University, Taichung, Taiwan, ROC;4. Department of Medical Research, Chung Shan Medical University Hospital, Taichung, Taiwan, ROC |
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| 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.Structured summary of protein interactionsPRMT1 binds to CNBP by pull down (View interaction)PRMT1 methylates CNBP by enzymatic study (View interaction)CNBP physically interacts with PRMT1 by anti tag coimmunoprecipitation (View interaction) |
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| Keywords: | CNBP RNA binding Protein arginine methylation |
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