Molecular characterization of the Entamoeba histolytica enolase gene and modelling of the predicted protein

María Eugenia Hidalgo; Roberto Sánchez; D. Guillermo Pérez; Mario A. Rodríguez; Job García; Esther Orozco

doi:10.1016/S0378-1097(96)00491-0

Molecular characterization of the Entamoeba histolytica enolase gene and modelling of the predicted protein

María Eugenia Hidalgo, Roberto Sánchez, D. Guillermo Pérez, Mario A. Rodríguez, Job García, Esther Orozco

Escuela Nacional de Medicina y Homeopatía (ENMH)

Research output: Contribution to journal › Article › peer-review

13 Scopus citations

Abstract

Entamoeba histolytica obtains its energy mainly from glucose fermentation. Enzymes involved in this pathway could be potential targets for antiparasite drugs. Here we report the molecular characterization of the E. histolytica enolase gene (Ehenl-1), which in a single copy is located on the 1.6 Mb chromosome. It is transcribed into a 1.4 kb mRNA which starts 13 nucleotides upstream of the ATG start codon. The sequence TATAAG, at -31, interacted with nuclear proteins suggesting that it has a TATA box function. Protein modelling allowed us to identify a putative specific region that differs from human enolase and could be a good target for the design of novel drugs against E. histolytica.

Original language	English
Pages (from-to)	123-129
Number of pages	7
Journal	FEMS Microbiology Letters
Volume	148
Issue number	2
DOIs	https://doi.org/10.1016/S0378-1097(96)00491-0
State	Published - 1997

Keywords

Entamoeba histolytica
chromosome mapping
enolase
protein modelling

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10.1016/S0378-1097(96)00491-0

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@article{fa34882c515d47d694ae2860b3a3d526,

title = "Molecular characterization of the Entamoeba histolytica enolase gene and modelling of the predicted protein",

abstract = "Entamoeba histolytica obtains its energy mainly from glucose fermentation. Enzymes involved in this pathway could be potential targets for antiparasite drugs. Here we report the molecular characterization of the E. histolytica enolase gene (Ehenl-1), which in a single copy is located on the 1.6 Mb chromosome. It is transcribed into a 1.4 kb mRNA which starts 13 nucleotides upstream of the ATG start codon. The sequence TATAAG, at -31, interacted with nuclear proteins suggesting that it has a TATA box function. Protein modelling allowed us to identify a putative specific region that differs from human enolase and could be a good target for the design of novel drugs against E. histolytica.",

keywords = "Entamoeba histolytica, chromosome mapping, enolase, protein modelling",

author = "Hidalgo, {Mar{\'i}a Eugenia} and Roberto S{\'a}nchez and {Guillermo P{\'e}rez}, D. and Rodr{\'i}guez, {Mario A.} and Job Garc{\'i}a and Esther Orozco",

note = "Funding Information: We are grateful to Dr. R. Arroyo for critical reading of the manuscript. Dr. E. Orozco is an International Fellow of Howard Hughes Medical Institute (USA). This work was also supported by CONACYT (M{\'e}xico), and INSERM (France).",

year = "1997",

doi = "10.1016/S0378-1097(96)00491-0",

language = "Ingl{\'e}s",

volume = "148",

pages = "123--129",

journal = "FEMS Microbiology Letters",

issn = "0378-1097",

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TY - JOUR

T1 - Molecular characterization of the Entamoeba histolytica enolase gene and modelling of the predicted protein

AU - Hidalgo, María Eugenia

AU - Sánchez, Roberto

AU - Guillermo Pérez, D.

AU - Rodríguez, Mario A.

AU - García, Job

AU - Orozco, Esther

N1 - Funding Information: We are grateful to Dr. R. Arroyo for critical reading of the manuscript. Dr. E. Orozco is an International Fellow of Howard Hughes Medical Institute (USA). This work was also supported by CONACYT (México), and INSERM (France).

PY - 1997

Y1 - 1997

N2 - Entamoeba histolytica obtains its energy mainly from glucose fermentation. Enzymes involved in this pathway could be potential targets for antiparasite drugs. Here we report the molecular characterization of the E. histolytica enolase gene (Ehenl-1), which in a single copy is located on the 1.6 Mb chromosome. It is transcribed into a 1.4 kb mRNA which starts 13 nucleotides upstream of the ATG start codon. The sequence TATAAG, at -31, interacted with nuclear proteins suggesting that it has a TATA box function. Protein modelling allowed us to identify a putative specific region that differs from human enolase and could be a good target for the design of novel drugs against E. histolytica.

AB - Entamoeba histolytica obtains its energy mainly from glucose fermentation. Enzymes involved in this pathway could be potential targets for antiparasite drugs. Here we report the molecular characterization of the E. histolytica enolase gene (Ehenl-1), which in a single copy is located on the 1.6 Mb chromosome. It is transcribed into a 1.4 kb mRNA which starts 13 nucleotides upstream of the ATG start codon. The sequence TATAAG, at -31, interacted with nuclear proteins suggesting that it has a TATA box function. Protein modelling allowed us to identify a putative specific region that differs from human enolase and could be a good target for the design of novel drugs against E. histolytica.

KW - Entamoeba histolytica

KW - chromosome mapping

KW - enolase

KW - protein modelling

UR - http://www.scopus.com/inward/record.url?scp=0030972336&partnerID=8YFLogxK

U2 - 10.1016/S0378-1097(96)00491-0

DO - 10.1016/S0378-1097(96)00491-0

M3 - Artículo

C2 - 9084139

AN - SCOPUS:0030972336

SN - 0378-1097

VL - 148

SP - 123

EP - 129

JO - FEMS Microbiology Letters

JF - FEMS Microbiology Letters

IS - 2

ER -

Molecular characterization of the Entamoeba histolytica enolase gene and modelling of the predicted protein

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Keywords

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