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

被引:18
作者
Figueroa-Angulo, Elisa E. [2 ]
Estrella-Hernandez, Priscila [1 ]
Salgado-Lugo, Holjes [1 ]
Ochoa-Leyva, Adrian [3 ]
Gomez Puyou, Armando [4 ]
Campos, Silvia S. [1 ]
Montero-Moran, Gabriela [1 ]
Ortega-Lopez, Jaime [5 ]
Saab-Rincon, Gloria [6 ]
Arroyo, Rossana [2 ]
Benitez-Cardoza, Claudia G. [7 ]
Brieba, Luis G. [1 ]
机构
[1] IPN, Ctr Invest & Estudios Avanzados, Lab Nacl Genom Biodiversidad, Irapuato, Guanajuato, Mexico
[2] IPN, Ctr Invest & Estudios Avanzados, Dept Infect & Patogenesis Mol, Mexico City 07360, DF, Mexico
[3] Inst Nacl Med Genom INMEGEN, Secretaria Salud, Mexico City 01900, DF, Mexico
[4] Univ Nacl Autonoma Mexico, Inst Fisiol Celular, Dept Bioquim & Biol Estruct, Mexico City 04510, DF, Mexico
[5] IPN, Ctr Invest & Estudios Avanzados, Dept Biotecnol & Bioingn, Mexico City 07360, DF, Mexico
[6] Univ Nacl Autonoma Mexico, Inst Biotecnol, Dept Ingn Celular & Biocatalisis, Cuernavaca 62210, Morelos, Mexico
[7] Inst Politecn Nacl, Programa Inst Biomed Mol ENMyH, Lab Invest Bioquim, La Escalera Ticoman 07320, DF, Mexico
关键词
duplicated gene; evolution; central metabolism; amitocondriate protozoa; structure-function; TRIOSE PHOSPHATE ISOMERASE; GIARDIA-LAMBLIA; GENE DUPLICATION; BINDING PROTEIN; CYSTEINE; INACTIVATION; GLUCOKINASE; INTERFACE; EVOLUTION; DISCOVERY;
D O I
10.1017/S003118201200114X
中图分类号
R38 [医学寄生虫学]; Q [生物科学];
学科分类号
07 ; 0710 ; 09 ; 100103 ;
摘要
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 alpha-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.
引用
收藏
页码:1729 / 1738
页数:10
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