title: Identification and functional characterization of lysine methyltransferases of Entamoeba histolytica.
abstract: Lysine methylation of histones, a posttranslational modification catalyzed by lysine methyltransferases (HKMTs), plays an important role in the epigenetic regulation of transcription. Lysine methylation of non-histone proteins also impacts the biological function of proteins. Previously it has been shown that lysine methylation of histones of Entamoeba histolytica, the protozoan parasite that infects 50 million people worldwide each year and causing up to 100,000 deaths annually, is implicated in the epigenetic machinery of this microorganism. However, the identification and characterization of HKMTs in this parasite had not yet been determined. In this work we identified four HKMTs in E. histolytica (EhHKMT1 to EhHKMT4) that are expressed by trophozoites. Enzymatic assays indicated that all of them are able to transfer methyl groups to commercial histones. EhHKMT1, EhHKMT2 and EhHKMT4 were detected in nucleus and cytoplasm of trophozoites. In addition EhHKMT2 and EhHKMT4 were located in vesicles containing ingested cells during phagocytosis, and they co-immunoprecipitated with EhADH, a protein involved in the phagocytosis of this parasite. Results suggest that E. histolytica uses its HKMTs to regulate transcription by epigenetic mechanisms, and at least two of them could also be implicated in methylation of proteins that participate in phagocytosis.
authors.affiliation: Departamento de Infectómica y Patogénesis Molecular. CINVESTAV-IPN. AP. 14-740 México, D.F. México.
authors.forename: Jessica
authors.initials: J
authors.lastname: Borbolla-Vázquez
authors.affiliation: Departamento de Infectómica y Patogénesis Molecular. CINVESTAV-IPN. AP. 14-740 México, D.F. México.
authors.forename: Esther
authors.initials: E
authors.lastname: Orozco
authors.affiliation: Departamento de Infectómica y Patogénesis Molecular. CINVESTAV-IPN. AP. 14-740 México, D.F. México.
authors.forename: Christian
authors.initials: C
authors.lastname: Medina-Gómez
authors.affiliation: Departamento de Infectómica y Patogénesis Molecular. CINVESTAV-IPN. AP. 14-740 México, D.F. México.
authors.forename: Aarón
authors.initials: A
authors.lastname: Martínez-Higuera
authors.affiliation: Departamento de Infectómica y Patogénesis Molecular. CINVESTAV-IPN. AP. 14-740 México, D.F. México.
authors.forename: Rosario
authors.initials: R
authors.lastname: Javier-Reyna
authors.affiliation: Departamento de Infectómica y Patogénesis Molecular. CINVESTAV-IPN. AP. 14-740 México, D.F. México.
authors.forename: Bibiana
authors.initials: B
authors.lastname: Chávez
authors.affiliation: Departamento de Infectómica y Patogénesis Molecular. CINVESTAV-IPN. AP. 14-740 México, D.F. México.
authors.forename: Abigail
authors.initials: A
authors.lastname: Betanzos
authors.affiliation: Departamento de Infectómica y Patogénesis Molecular. CINVESTAV-IPN. AP. 14-740 México, D.F. México.
authors.forename: Mario A
authors.initials: MA
authors.lastname: Rodríguez
mesh_terms: D000595:Amino Acid Sequence; D004748:Entamoeba histolytica / Q000235:genetics / Q000378:metabolism*; D044127:Epigenesis, Genetic / Q000235:genetics; D006657:Histones / Q000378:metabolism*; D008239:Lysine / Q000378:metabolism; D008745:Methylation; D008780:Methyltransferases / Q000378:metabolism*; D011499:Protein Processing, Post-Translational / Q000235:genetics; D053058:Trophozoites / Q000378:metabolism
chemical_list: D006657:Histones; D008780:Methyltransferases; D008239:Lysine