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Arginine Methylation of Recombinant Murine Fibrillarin by Protein Arginine Methyltransferase

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Abstract

Fibrillarin is a conserved nucleolar SnoRNP with a diverse N-terminal glycine- and arginine-rich (GAR) domain in most eukaryotes. This region in human fibrillarin is known to contain modified dimethylarginines. In this report we demonstrate that recombinant murine fibrillarin is a substrate for protein arginine methyltransferase, including the purified recombinant enzyme (rat PRMT1 and yeast RMT1) and the protein methyltransferases present in lymphoblastoid cell extracts. Our results of protease digestion, methylation competition reactions, and immunoblotting with a methylarginine-specific antibody all indicate that the methylation of fibrillarin is in the N-terminal GAR domain and arginyl residues are modified. Finally, amino acid analyses revealed that the modification of recombinant murine fibrillarin forms methylarginines, mostly as dimethylarginines.

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Authors and Affiliations

  1. Institute of Medicine, Chung Shan Medical and Dental University, Taichung, China

    Chia-Hui Lin & Hung-Ming Huang

  2. Department of Life Science, Chung Shan Medical and Dental University, Taichung, China

    Mingli Hsieh & Chuan Li

  3. W. M. Keck Autoimmune Disease Center, Department of Molecular and Experimental Medicine, The Scripps Research Institute, 10550 North Torrey Pines Road, La Jolla, California, 92037

    K. Michael Pollard

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  1. Chia-Hui Lin
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  2. Hung-Ming Huang
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  3. Mingli Hsieh
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  5. Chuan Li
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Correspondence to Chuan Li.

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Lin, CH., Huang, HM., Hsieh, M. et al. Arginine Methylation of Recombinant Murine Fibrillarin by Protein Arginine Methyltransferase. J Protein Chem 21, 447–453 (2002). https://doi.org/10.1023/A:1021394903025

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