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Eukaryotic Cell, September 2007, p. 1665-1681, Vol. 6, No. 9
1535-9778/07/$08.00+0     doi:10.1128/EC.00133-07
Copyright © 2007, American Society for Microbiology. All Rights Reserved.

Evolutionarily Divergent Type II Protein Arginine Methyltransferase in Trypanosoma brucei{triangledown}

Deborah A. Pasternack,1 Joyce Sayegh,2 Steven Clarke,2 and Laurie K. Read1*

Department of Microbiology and Immunology and Witebsky Center for Microbial Pathogenesis and Immunology, State University of New York School of Medicine, Buffalo, New York 14214,1 Department of Chemistry and Biochemistry and Molecular Biology Institute, University of California at Los Angeles, Los Angeles, California 90095-15692

Received 20 April 2007/ Accepted 22 June 2007

Protein arginine methylation is a posttranslational modification that impacts cellular functions, such as RNA processing, transcription, DNA repair, and signal transduction. The majority of our knowledge regarding arginine methylation derives from studies of yeast and mammals. Here, we describe a protein arginine N-methyltransferase (PRMT), TbPRMT5, from the early-branching eukaryote Trypanosoma brucei. TbPRMT5 shares the greatest sequence similarity with PRMT5 and Skb1 type II enzymes from humans and Schizosaccharomyces pombe, respectively, although it is significantly divergent at the amino acid level from its mammalian and yeast counterparts. Recombinant TbPRMT5 displays broad substrate specificity in vitro, including methylation of a mitochondrial-gene-regulatory protein, RBP16. TbPRMT5 catalyzes the formation of {omega}-NG-monomethylarginine and symmetric {omega}-NG,NG'-dimethylarginine and does not require trypanosome cofactors for this activity. These data establish that type II PRMTs evolved early in the eukaryotic lineage. In vivo, TbPRMT5 is constitutively expressed in the bloodstream form and procyclic-form (insect host) life stages of the parasite and localizes to the cytoplasm. Genetic disruption via RNA interference in procyclic-form trypanosomes indicates that TbPRMT5 is not essential for growth in this life cycle stage. TbPRMT5-TAP ectopically expressed in procyclic-form trypanosomes is present in high-molecular-weight complexes and associates with an RG domain-containing DEAD box protein related to yeast Ded1 and two kinetoplastid-specific proteins. Thus, TbPRMT5 is likely to be involved in novel methylation-regulated functions in trypanosomes, some of which may include RNA processing and/or translation.

* Corresponding author. Mailing address: Department of Microbiology and Immunology, SUNY Buffalo School of Medicine, 138 Farber Hall, Buffalo, NY 14214. Phone: (716) 829-3307. Fax: (716) 829-2158. E-mail: lread{at}acsu.buffalo.edu

{triangledown} Published ahead of print on 29 June 2007.

Eukaryotic Cell, September 2007, p. 1665-1681, Vol. 6, No. 9
1535-9778/07/$08.00+0     doi:10.1128/EC.00133-07
Copyright © 2007, American Society for Microbiology. All Rights Reserved.



This article has been cited by other articles:

  • Shi, H., Chamond, N., Djikeng, A., Tschudi, C., Ullu, E. (2009). RNA Interference in Trypanosoma brucei: ROLE OF THE N-TERMINAL RGG DOMAIN AND THE POLYRIBOSOME ASSOCIATION OF ARGONAUTE. J. Biol. Chem. 284: 36511-36520 [Abstract] [Full Text]  
  • Fisk, J. C., Presnyak, V., Ammerman, M. L., Read, L. K. (2009). Distinct and Overlapping Functions of MRP1/2 and RBP16 in Mitochondrial RNA Metabolism. Mol. Cell. Biol. 29: 5214-5225 [Abstract] [Full Text]  
  • Fisk, J. C., Sayegh, J., Zurita-Lopez, C., Menon, S., Presnyak, V., Clarke, S. G., Read, L. K. (2009). A Type III Protein Arginine Methyltransferase from the Protozoan Parasite Trypanosoma brucei. J. Biol. Chem. 284: 11590-11600 [Abstract] [Full Text]  


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