http://192.168.1.40:8080/xmlui/handle/123456789/1128 Sun, 31 May 2026 13:43:11 GMT 2026-05-31T13:43:11Z http://192.168.1.40:80/xmlui/bitstream/id/ad35ef8c-559d-4556-a97f-386082a6e026/anuradha1.jpg http://192.168.1.40:8080/xmlui/handle/123456789/1128 http://192.168.1.40:8080/xmlui/handle/123456789/2336 The genome of the protist parasite Entamoeba histolytica Loftus, B.; Lohia, Anuradha Entamoeba histolytica is an intestinal parasite and the causative agent of amoebiasis, which is a significant source of morbidity and mortality in developing countries(1). Here we present the genome of E. histolytica, which reveals a variety of metabolic adaptations shared with two other amitochondrial protist pathogens: Giardia lamblia and Trichomonas vaginalis. These adaptations include reduction or elimination of most mitochondrial metabolic pathways and the use of oxidative stress enzymes generally associated with anaerobic prokaryotes. Phylogenomic analysis identifies evidence for lateral gene transfer of bacterial genes into the E. histolytica genome, the effects of which centre on expanding aspects of E. histolytica's metabolic repertoire. The presence of these genes and the potential for novel metabolic pathways in E. histolytica may allow for the development of new chemotherapeutic agents. The genome encodes a large number of novel receptor kinases and contains expansions of a variety of gene families, including those associated with virulence. Additional genome features include an abundance of tandemly repeated transfer-RNA-containing arrays, which may have a structural function in the genome. Analysis of the genome provides new insights into the workings and genome evolution of a major human pathogen. DOI: 10.1038/nature03291 Thu, 24 Feb 2005 00:00:00 GMT http://192.168.1.40:8080/xmlui/handle/123456789/2336 2005-02-24T00:00:00Z http://192.168.1.40:8080/xmlui/handle/123456789/2317 Entamoeba histolytica DNA methyltransferase (Ehmeth) is a nuclear matrix protein that binds EhMRS2, a DNA that includes a scaffold/matrix attachment region (S/MAR) Banerjee, S.; Fisher, O.; Lohia, Anuradha; Ankri, S. The protozoan parasite Entamoeba histolytica express a cytosine-5 DNA methyltransferase (Ehmeth) that belongs to the DNMT2 protein family. The biological function of members of this DNMT2 family is unknown. In the present study, we have demonstrated that Ehmeth is a nuclear matrix protein. Indeed, we showed by south-western analysis and yeast one-hybrid system that Ehmeth binds to EhMRS2, a DNA element which contains the eukaryotic consensus scaffold/inatrix attachment regions (S/MAR) bipartite recognition sequences. S/MARs have been implicated in a variety of important functions, such as genome organization and gene expression. The methylation status of cytosine located within EhMRS2 was analyzed by bisulfite genomic sequencing. We observed the presence of methylated cytosine within the 3'-end of EhMRS2. These data provide the first evidence that a member of the DNMT2 family interacts with a S/MAR containing DNA element. DOI: 10.1016/j.molbiopara.2004.10.003 Sat, 01 Jan 2005 00:00:00 GMT http://192.168.1.40:8080/xmlui/handle/123456789/2317 2005-01-01T00:00:00Z http://192.168.1.40:8080/xmlui/handle/123456789/2314 Inhibition of gene expression with double strand RNA interference in Entamoeba histolytica Kaur, G.; Lohia, Anuradha In order to inhibit gene expression in Entamoeba histolytica, we have developed a method based on expressing double strand RNA interference constructs in stable transformants. The 5' end of Eh Dia was cloned head to head with an intervening non-specific stuffer fragment in the E. histolytica expression vector pJST4. This construct was transformed in E. histolytica HM1:IMSS trophozoites and stable transformants were selected with 20 mug/ml G418. Our results show that expression of Eh Dia was completely inhibited in these transformants. These stable transformants could be maintained indefinitely without expression of Eh Dia. This method therefore provides an effective tool to study the phenotypic changes, which occur due to inhibition of gene expression in the absence of mutants and other microbiological manipulations in this protozoan parasite. DOI: 10.1016/j.bbrc.2004.06.064 Fri, 06 Aug 2004 00:00:00 GMT http://192.168.1.40:8080/xmlui/handle/123456789/2314 2004-08-06T00:00:00Z http://192.168.1.40:8080/xmlui/handle/123456789/2312 The Iml3 protein of the budding yeast is required for the prevention of precocious sister chromatid separation in meiosis I and for sister chromatid disjunction in meiosis II Ghosh, S. K.; Sau, S.; Lahiri, S.; Lohia, Anuradha; Sinha, Pratima The mitotic kinetochore of the budding yeast contains a number of proteins which are required for chromosome transmission but are non-essential for vegetative growth. We show that one such protein, Iml3, is essential for meiosis, in that the absence of this protein results in reduced spore viability, precocious sister chromatid segregation of artificial and natural chromosomes in meiosis I and chromosome non-disjunction in meiosis II. DOI: 10.1007/s00294-004-0516-6 Sun, 01 Aug 2004 00:00:00 GMT http://192.168.1.40:8080/xmlui/handle/123456789/2312 2004-08-01T00:00:00Z