Abstract:
: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.
journal_name
Parasitologyjournal_title
Parasitologyauthors
Figueroa-Angulo EE,Estrella-Hernández P,Salgado-Lugo H,Ochoa-Leyva A,Gómez Puyou A,Campos SS,Montero-Moran G,Ortega-López J,Saab-Rincón G,Arroyo R,Benítez-Cardoza CG,Brieba LGdoi
10.1017/S003118201200114Xsubject
Has Abstractpub_date
2012-11-01 00:00:00pages
1729-38issue
13eissn
0031-1820issn
1469-8161pii
S003118201200114Xjournal_volume
139pub_type
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