BackgroundIn eukaryotes, histone arginine methylation associates with both active and repressed chromatin states depending on the residues involved and the status of methylation. Even when the amino-terminus of Entamoeba histolytica histones diverge from metazoan sequences, these regions contain arginine residues that are potential targets for methylation. However, histone arginine methylation as well as the activity of arginine methyltransferases (PRMTs) has not been studied in this parasite. The aim of this work was to examine the dimethylation of arginine 3 of H4 histone (H4R3me2) and to identify the parasite PRMT that could be responsible for this modification (EhPRMT1).MethodsTo examine the presence of H4R3me2 in E histolytica, we performed Western blot and immunofluorescence assays on trophozoites using an antibody against this epigenetic mark. To recognize the PRMT1 enzyme of this parasite that possibly perform that modification, we first performed a phylogenetic analysis of E. histolytica and human PRMTs. RT-PCR assays were carried out to analyze the expression of the putative PRMT1 genes. One of these genes was cloned and expressed in Escherichia coli. The recombinant protein was tested by its recognition by an antibody against human PRMT1 and in its ability to form homodimers and to methylate commercial histones.ResultsThe arginine 3 of human H4, which is subjected to post translational methylation, was aligned with the arginine 8 of E. histolytica H4, suggesting that this residue could be methylated. The recognition of an 18 kDa nuclear protein of E. histolytica by an antibody against H4R3me2 confirmed this assumption. We found that this parasite expresses three phylogenetic and structural proteins related to PRMT1. Antibodies against the human PRMT1 detected E. histolytica proteins in cytoplasm and nuclei and recognized a recombinant PRMT1 of this parasite. The recombinant protein was able to form homodimers and homotetramers and displayed methyltransferase activity on arginine 3 of chicken H4.ConclusionAll these results suggest that E. histolytica contains as a minimum one structural and functional protein ortholog to PRMT1, enzyme that potentially dimethylates H4R8. This modification may play an important role in the gene expression regulation of this microorganism.

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.

The large increase in population in Cancun, Mexico has increased domestic, agricultural and industrial activities, resulting in inadequate solid and liquid waste management that can affect underground aquifers. One of the factors which affects water quality is coliform bacteria. The present study focused on determining the presence of total and faecal coliforms in ten urban cenotes in Cancun. Sampling was carried out in the dry and rainy seasons of 2018. The Most Probable Number (MPN) technique was used to determine the concentration of coliform bacteria. The results from the analyses indicate that the ten cenotes are contaminated with total and faecal coliforms. Additionally, the concentration of coliforms increases during the rainy season. We conclude that all the cenotes are contaminated with faecal coliforms and suggest that more studies are necessary to determine the origin of this contamination and the impact on the ecosystem.

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Organic coffee and orange wastes have increased considerably in the last decade. In order to utilize this "garbage", the present study focuses on the obtaining of activated carbon from them. The pyrolysis of the samples, followed by chemical activation and subsequent neutralization, allowed the establishment of two protocols “A” and “B”, with slight variations depending on the residue. The results indicate that the efficiency of the activated carbon from coffee grounds using protocol "A" and "B" was 3.68% and 6.30%, respectively. On the other hand, the carbon obtained from orange peels had an efficiency of 5.00 % and 2.88 %, respectively. To confirm that the activated carbon from each type of waste has adsorption and absorption capacity, we performed a colorimetric analysis with methyl blue. These analyses showed that the activated carbon from coffee grounds and orange peels have a retention capacity of 91.09 and 95.25%, respectively, while the retention capacity of a commercial activated carbon was 99.23 %. In this preliminary study, it is shown that several residues considered "garbage" can be used sustainably.

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