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Cellular and biochemical characterization of two closely related triosephosphate isomerases from Trichomonas vaginalis

Published online by Cambridge University Press:  29 August 2012

ELISA E. FIGUEROA-ANGULO ,
PRISCILA ESTRELLA-HERNÁNDEZ ,
HOLJES SALGADO-LUGO ,
ADRIÁN OCHOA-LEYVA ,
ARMANDO GÓMEZ PUYOU ,
SILVIA S. CAMPOS ,
GABRIELA MONTERO-MORAN ,
JAIME ORTEGA-LÓPEZ ,
GLORIA SAAB-RINCÓN  and
ROSSANA ARROYO
...Show all authors
ELISA E. FIGUEROA-ANGULO
Affiliation:
Departamento de Infectómica y Patogénesis Molecular, Centro de Investigación y de Estudios Avanzados del IPN, Col. San Pedro Zacatenco, Av. IPN, 2508, C.P. 07360, México, D.F.
PRISCILA ESTRELLA-HERNÁNDEZ
Affiliation:
Laboratorio Nacional de Genómica para la Biodiversidad, Centro de Investigación y de Estudios Avanzados del IPN, Km. 9·6 Libramiento Norte Carr. Irapuato-León 36821, Irapuato, Guanajuato, México
HOLJES SALGADO-LUGO
Affiliation:
Laboratorio Nacional de Genómica para la Biodiversidad, Centro de Investigación y de Estudios Avanzados del IPN, Km. 9·6 Libramiento Norte Carr. Irapuato-León 36821, Irapuato, Guanajuato, México
ADRIÁN OCHOA-LEYVA
Affiliation:
Instituto Nacional de Medicina Genómica (INMEGEN), Secretaría de Salud, México City, Distrito Federal, C.P. 01900, México
ARMANDO GÓMEZ PUYOU
Affiliation:
Departamento de Bioquímica y Biología Estructural, Instituto de Fisiología Celular, Universidad Nacional Autónoma de México, Mexico City, México
SILVIA S. CAMPOS
Affiliation:
Laboratorio Nacional de Genómica para la Biodiversidad, Centro de Investigación y de Estudios Avanzados del IPN, Km. 9·6 Libramiento Norte Carr. Irapuato-León 36821, Irapuato, Guanajuato, México
GABRIELA MONTERO-MORAN
Affiliation:
Laboratorio Nacional de Genómica para la Biodiversidad, Centro de Investigación y de Estudios Avanzados del IPN, Km. 9·6 Libramiento Norte Carr. Irapuato-León 36821, Irapuato, Guanajuato, México
JAIME ORTEGA-LÓPEZ
Affiliation:
Departamento de Biotecnología y Bioingeniería, Centro de Investigación y de Estudios Avanzados del IPN, Col. San Pedro Zacatenco, Av. IPN, 2508, C.P. 07360, México, D.F.
GLORIA SAAB-RINCÓN
Affiliation:
Departamento de Ingeniería Celular y Biocatálisis, Instituto de Biotecnología, Universidad Nacional Autónoma de México, Avenida Universidad 2001, Cuernavaca, C.P. 62210, México
ROSSANA ARROYO
Affiliation:
Departamento de Infectómica y Patogénesis Molecular, Centro de Investigación y de Estudios Avanzados del IPN, Col. San Pedro Zacatenco, Av. IPN, 2508, C.P. 07360, México, D.F.
CLAUDIA G. BENÍTEZ-CARDOZA
Affiliation:
Laboratorio de Investigación Bioquímica, Programa Institucional en Biomedicina Molecular ENMyH-Instituto Politécnico Nacional, Guillermo Massieu Helguera No. 239, La Escalera Ticomán, 07320, D.F, México
LUIS G. BRIEBA*
Affiliation:
Laboratorio Nacional de Genómica para la Biodiversidad, Centro de Investigación y de Estudios Avanzados del IPN, Km. 9·6 Libramiento Norte Carr. Irapuato-León 36821, Irapuato, Guanajuato, México
*
*Corresponding author: Laboratorio Nacional de Genómica para la Biodiversidad, Centro de Investigación y de Estudios Avanzados del IPN, Km. 9·6 Libramiento Norte Carr. Irapuato-León 36821, Irapuato, Guanajuato, México. E-mail: lgbrieba@ira.cinvestav.mx
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Summary

The glycolytic enzyme triosephosphate isomerase catalyses the isomerization between glyceraldehyde 3-phosphate and dihydroxyacetone phosphate. Here we report that Trichomonas vaginalis contains 2 fully functional tpi genes. Both genes are located in separated chromosomal context with different promoter regulatory elements and encode ORFs of 254 amino acids; the only differences between them are the character of 4 amino acids located in α-helices 1, 2 and 8. Semi-quantitative RT-PCR assays showed that tpi2 transcript is approximately 3·3-fold more abundant than tpi1. Using an anti-TvTIM2 polyclonal antibody it was demonstrated that TIM proteins have a cytoplasmic localization and both enzymes are able to complement an Escherichia coli strain carrying a deletion of its endogenous tpi gene. Both TIM proteins assemble as dimers and their secondary structure assessment is essentially identical to TIM from Saccharomyces cerevisiae. The kinetic catalytic constants of the recombinant enzymes using glyceraldehyde-3-phosphate as substrate are similar to the catalytic constants of TIMs from other organisms including parasitic protozoa. As T. vaginalis depends on glycolysis for ATP production, we speculate 2 possible reasons to maintain a duplicated tpi copy on its genome: an increase in gene dosage or an early event of neofunctionalization of TIM as a moonlighting protein.

Keywords

duplicated geneevolutioncentral metabolismamitocondriate protozoastructure-function
Type
Research Article
Information
Parasitology , Volume 139 , Issue 13 , November 2012 , pp. 1729 - 1738
Copyright
Copyright © Cambridge University Press 2012

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