Parasites, Hosts and Diseases

The Korea Society for Parasitology and Tropical Medicine (대한기생충학·열대의학회)
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Identification and Characterization of Protein Arginine Methyltransferase 1 in Acanthamoeba castellanii

  • Moon, Eun-Kyung (Department of Medical Zoology, Kyung Hee University School of Medicine) ;
  • Kong, Hyun-Hee (Department of Parasitology, Dong-A University College of Medicine) ;
  • Hong, Yeonchul (Department of Parasitology and Tropical Medicine, Kyungpook National University School of Medicine) ;
  • Lee, Hae-Ahm (Department of Pharmacology, Kyungpook National University School of Medicine) ;
  • Quan, Fu-Shi (Department of Medical Zoology, Kyung Hee University School of Medicine)
  • Received : 2017.02.06
  • Accepted : 2017.04.08
  • Published : 2017.04.30
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Abstract

Protein arginine methyltransferase (PRMT) is an important epigenetic regulator in eukaryotic cells. During encystation, an essential process for Acanthamoeba survival, the expression of a lot of genes involved in the encystation process has to be regulated in order to be induced or inhibited. However, the regulation mechanism of these genes is yet unknown. In this study, the full-length 1,059 bp cDNA sequence of Acanthamoeba castellanii PRMT1 (AcPRMT1) was cloned for the first time. The AcPRMT1 protein comprised of 352 amino acids with a SAM-dependent methyltransferase PRMT-type domain. The expression level of AcPRMT1 was highly increased during encystation of A. castellanii. The EGFP-AcPRMT1 fusion protein was distributed over the cytoplasm, but it was mainly localized in the nucleus of Acanthamoeba. Knock down of AcPRMT1 by synthetic siRNA with a complementary sequence failed to form mature cysts. These findings suggested that AcPRMT1 plays a critical role in the regulation of encystation of A. castellanii. The target gene of AcPRMT1 regulation and the detailed mechanisms need to be investigated by further studies.

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References

  1. Marciano-Cabral F, Cabral G. Acanthamoeba spp. as agents of disease in humans. Clin Microbiol Rev 2003; 16: 273-307. https://doi.org/10.1128/CMR.16.2.273-307.2003
  2. Moon EK, Xuan YH, Chung DI, Hong Y, Kong HH. Microarray analysis of differentially expressed genes between cysts and trophozoites of Acanthamoeba castellanii. Korean J Parasitol 2011; 49: 341-347. https://doi.org/10.3347/kjp.2011.49.4.341
  3. Portela A, Esteller M. Epigenetic modifications and human disease. Nat Biotechnol 2010; 28: 1057-1068. https://doi.org/10.1038/nbt.1685
  4. Kirmizis A, Santos-Rosa H, Penkett CJ, Singer MA, Vermeulen M, Mann M, Bahler J, Green RD, Kouzarides T. Arginine methylation at histone H3R2 controls deposition of H3K4 trimethylation. Nature 2007; 449: 928-932. https://doi.org/10.1038/nature06160
  5. Bedford MT, Clarke SG. Protein arginine methylation in mammals: who, what, and why. Mol Cell 2009; 33: 1-13. https://doi.org/10.1016/j.molcel.2008.12.013
  6. Pahlich S, Zakaryan RP, Gehring H. Protein arginine methylation: cellular functions and methods of analysis. Biochim Biophys Acta 2006; 1764: 1890-1903. https://doi.org/10.1016/j.bbapap.2006.08.008
  7. Niewmierzycka A, Clarke S. S-adenosylmethionine-dependent methylation in Saccharomyces cerevisiae. Identification of a novel protein arginine methyltransferase. J Biol Chem 1999; 274: 814-824. https://doi.org/10.1074/jbc.274.2.814
  8. Pawlak MR, Scherer CA, Chen J, Roshon MJ, Ruley HE. Arginine N-methyltransferase 1 is required for early postimplantation mouse development, but cells deficient in the enzyme are viable. Mol Cell Biol 2000; 20: 4859-4869. https://doi.org/10.1128/MCB.20.13.4859-4869.2000
  9. Krause CD, Yang ZH, Kim YS, Lee JH, Cook JR, Pestka S. Protein arginine methyltransferases: evolution and assessment of their pharmacological and therapeutic potential. Pharmacol Ther 2007; 113: 50-87. https://doi.org/10.1016/j.pharmthera.2006.06.007
  10. Katsanis N, Yaspo ML, Fisher EM. Identification and mapping of a novel human gene, HRMT1L1, homologous to the rat protein arginine N-methyltransferase 1 (PRMT1) gene. Mamm Genome 1997; 8: 526-529. https://doi.org/10.1007/s003359900491
  11. Nicholson TB, Chen T, Richard S. The physiological and pathophysiological role of PRMT1-mediated protein arginine methylation. Pharmacol Res 2009; 60: 466-474. https://doi.org/10.1016/j.phrs.2009.07.006
  12. Kraus WL, Wong J. Nuclear receptor-dependent transcription with chromatin. Is it all about enzymes? Eur J Biochem 2002; 269: 2275-2283. https://doi.org/10.1046/j.1432-1033.2002.02889.x
  13. Fan Q, Miao J, Cui L, Cui L. Characterization of PRMT1 from Plasmodium falciparum. Biochem J 2009; 421: 107-118. https://doi.org/10.1042/BJ20090185
  14. Borbolla-Vazquez J, Orozco E, Betanzos A, Rodriguez MA. Entamoeba histolytica: protein arginine transferase 1a methylates arginine residues and potentially modify the H4 histone. Parasit Vectors 2015; 8: 219. https://doi.org/10.1186/s13071-015-0820-7
  15. Bowers B, Korn ED. The fine structure of Acanthamoeba castellanii (Neff strain). II. Encystment. J Cell Biol 1969; 41: 786-805. https://doi.org/10.1083/jcb.41.3.786
  16. Aqeel Y, Siddiqui R, Khan NA. Silencing of xylose isomerase and cellulose synthase by siRNA inhibits encystation in Acanthamoeba castellanii. Parasitol Res 2013; 112: 1221-1127. https://doi.org/10.1007/s00436-012-3254-6
  17. Moon EK, Hong Y, Chung DI, Kong HH. Cysteine protease involving in autophagosomal degradation of mitochondria during encystation of Acanthamoeba. Mol Biochem Parasitol 2012; 185: 121-126. https://doi.org/10.1016/j.molbiopara.2012.07.008
  18. Livak KJ, Schmittgen TD. Analysis of relative gene expression data using real-time quantitative PCR and the 2(-Delta Delta C(T)) Method. Methods 2001; 25: 402-408. https://doi.org/10.1006/meth.2001.1262
  19. Moon EK, Hong Y, Chung DI, Goo YK, Kong HH. Identification of protein arginine methyltransferase 5 as a regulator for encystation of Acanthamoeba. Korean J Parasitol 2016; 54: 133-1338. https://doi.org/10.3347/kjp.2016.54.2.133
  20. Litt M, Qiu Y, Huang S. Histone arginine methylations: their roles in chromatin dynamics and transcriptional regulation. Biosci Rep 2009; 29: 131-141. https://doi.org/10.1042/BSR20080176
  21. Di Lorenzo A, Bedford MT. Histone arginine methylation. FEBS Lett 2011; 585: 2024-2031. https://doi.org/10.1016/j.febslet.2010.11.010
  22. Mansure JJ, Furtado DR, de Oliveira FM, Rumjanek FD, Franco GR, Fantappie MR. Cloning of a protein arginine methyltransferase PRMT1 homologue from Schistosoma mansoni: evidence for roles in nuclear receptor signaling and RNA metabolism. Biochem Biophys Res Commun 2005; 335: 1163-1172. https://doi.org/10.1016/j.bbrc.2005.07.192
  23. Wang H, Huang ZQ, Xia L, Feng Q, Erdjument-Bromage H, Strahl BD, Briggs SD, Allis CD, Wong J, Tempst P, Zhang Y. Methylation of histone H4 at arginine 3 facilitating transcriptional activation by nuclear hormone receptor. Science 2001; 293: 853-857. https://doi.org/10.1126/science.1060781
  24. Pal S, Vishwanath SN, Erdjument-Bromage H, Tempst P, Sif S. Human SWI/SNF-associated PRMT5 methylates histone H3 arginine 8 and negatively regulates expression of ST7 and NM23 tumor suppressor genes. Mol Cell Biol 2004; 24: 9630-9645. https://doi.org/10.1128/MCB.24.21.9630-9645.2004

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