Structural and functional analysis of the Entamoeba histolytica EhrabB gene promoter

Romero-Díaz, Mónica; Gómez, Consuelo; López-Reyes, Israel; Martínez, Máximo B.; Orozco, Esther; Rodríguez, Mario A.

doi:10.1186/1471-2199-8-82

Cited by 22 publications

(28 citation statements)

References 41 publications

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“…Whereas we found the GAAC box and the alternative Inr element, we did not find the TATA box and Inr element sequence in most of the RING E3s. Absence of these elements has been shown for other Entamoeba genes and it is also known that AT rich sequences of six base pairs or more can substitute for TATA activity in association with other control elements (Gómez et al 1998;Purdy et al 1996;Romero-Díaz et al 2010). Other than these known motifs, a number of motifs were identified with significant e-values (Online Resource 13).…”

Section: Discussionmentioning

confidence: 99%

In silico analysis of ubiquitin/ubiquitin-like modifiers and their conjugating enzymes in Entamoeba species

et al. 2012

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Covalent modification of proteins by ubiquitin (Ub) and ubiquitin-like modifiers (Ubls) regulates many cellular functions in eukaryotes. These modifications are likely to be associated with pathogenesis, growth, and development of many protozoan parasites but molecular details about this pathway are unavailable for most protozoa. This study presents an analysis of the Ub pathway in three members of the Entamoeba species. Using bioinformatics tools we have identified all Ub and Ubl genes along with their corresponding activating, conjugating, and ligating enzymes (E1, E2s, and E3s) in three Entamoeba species, Entamoeba histolytica, Entamoeba dispar, and Entamoeba invadens. Phylogenetic trees were established for the identified E2s and RING finger E3s using maximum-likelihood method to infer the relationship among these proteins. In silico co-domain analysis of RING finger E3s implicates these proteins in a variety of functions. Several known and putative regulatory motifs were identified in the upstream regions of RING finger domain containing E3 genes. All E2 and E3 genes were analyzed in genomic context in E. histolytica and E. dispar. Most E2s and E3s were in syntenic positions in the two genomes. Association of these genes with transposable elements (TEs) was compared between E. histolytica and E. dispar. A closer association was found between RING finger E3s with TEs in E. histolytica. In summary, our analyses suggests that the complexity of the Ub pathway in Entamoeba species is close to that observed in higher eukaryotes. This study provides important data for further understanding the role of Ub pathway in the biology of these organisms.

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Section: Discussionmentioning

confidence: 99%

In silico analysis of ubiquitin/ubiquitin-like modifiers and their conjugating enzymes in Entamoeba species

et al. 2012

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“…The EhrabB gene is located in the complementary chain of the DNA fragment containing the Ehcp112 and Ehadh genes (Juarez‐Hernandez et al, ; Rodriguez et al, ). Furthermore, their regulatory sequences overlap (Flores‐Soto, Azuara‐Liceaga, Lopez‐Camarillo, & Orozco, ; Romero‐Diaz et al, ). Organisation of EhrabB , Ehcp112 , and Ehadh genes in the genome could suggest that the roles of the encoding proteins may be somehow linked; however, the functional relationship of the three proteins is not well known.…”

Section: Introductionmentioning

confidence: 99%

EhRabB mobilises the EhCPADH complex through the actin cytoskeleton during phagocytosis of Entamoeba histolytica

Javier-Reyna

Montaño

Garcı́a-Rivera

et al. 2019

Cellular Microbiology

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Movement and phagocytosis are clue events in colonisation and invasion of tissues by Entamoeba histolytica, the protozoan causative of human amoebiasis. During phagocytosis, EhRab proteins interact with other functional molecules, conducting them to the precise cellular site. The gene encoding EhrabB is located in the complementary chain of the DNA fragment containing Ehcp112 and Ehadh genes, which encode for the proteins of the EhCPADH complex, involved in phagocytosis. This particular genetic organisation suggests that the three corresponding proteins may be functionally related. Here, we studied the relationship of EhRabB with EhCPADH and actin during phagocytosis. First, we obtained the EhRabB 3D structure to carry out docking analysis to predict the interaction sites involved in the EhRabB protein and the EhCPADH complex contact. By confocal microscopy, transmission electron microscopy, and immunoprecipitation assays, we revealed the interaction among these proteins when they move through different vesicles formed during phagocytosis. The role of the actin cytoskeleton in this event was also confirmed using Latrunculin A to interfere with actin polymerisation. This affected the movement of EhRabB and EhCPADH, as well as the rate of phagocytosis. Mutant trophozoites, silenced in EhrabB gene, evidenced the interaction of this molecule with EhCPADH and strengthened the role of actin during erythrophagocytosis.

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“…This 33 bp DNA fragment contains the only inverse repeat (TTC) of HSE that was found in the 5′ non-coding region of EhMLBP in addition to the repeats of the sequence GAA thus making this region to contain a perfect triplicate of HSE. The presence of HSEs has been reported in the promoter region of proteins that are not HSPs, such as interleukin-6 (A.A. Parikh, 1988), p35 (Chang et al, 2006) and E. histolytica Rab GTPase (Romero-Diaz et al, 2007). The results of a recent analysis on the whole-genome sequence of Drosophila melanogaster showed that only 10% of the genes that contain HSE are indeed upregulated by HS (Gonsalves et al, 2011).…”

Section: Ehmlbp Expression Is Regulated By Hsmentioning

confidence: 99%

The Entamoeba histolytica methylated LINE-binding protein EhMLBP provides protection against heat shock

Katz

Kushnir

Tovy

et al. 2011

Cellular Microbiology

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SummaryAdaptation to environmental stress is a key process that allows the unicellular parasite Entamoeba histolytica to survive in its human host. We previously characterized EhMLBP as an essential protein for the growth and the virulence of the parasite. EhMLBP binds to methylated repetitive DNA, and is one of the core proteins of the parasite's epigenetic machinery. Here, we show that EhMLBP and heat shock proteins have common properties. EhMLBP is induced by heat shock and its expression is regulated by a heat shock element binding site that is located in its 5Ј noncoding region. Following heat shock, the perinuclear localization of EhMLBP in control trophozoites is replaced by an even distribution within the nucleus alongside with an enhanced recruitment of EhMLBP to the reverse transcriptase of a long interspersed nucleotide element (LINE) DNA. Constitutive overexpression of EhMLBP protects trophozoites against heat shock and reduces protein aggregation. This protective function is lost in trophozoites that overexpress a mutated form of EhMLBP which is devoid of its heat shock domain. To the best of our knowledge, this is the first report of a methyl DNAbinding protein that plays a protective role against heat shock.

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Structural and functional analysis of the Entamoeba histolytica EhrabB gene promoter

Cited by 22 publications

References 41 publications

In silico analysis of ubiquitin/ubiquitin-like modifiers and their conjugating enzymes in Entamoeba species

In silico analysis of ubiquitin/ubiquitin-like modifiers and their conjugating enzymes in Entamoeba species

EhRabB mobilises the EhCPADH complex through the actin cytoskeleton during phagocytosis of Entamoeba histolytica

The Entamoeba histolytica methylated LINE-binding protein EhMLBP provides protection against heat shock

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