Biogenesis of the hydrogenosome in the anaerobic protist Trichomonas vaginalis - PubMed (original) (raw)

Affiliations

PMID: 8410536

Review

Biogenesis of the hydrogenosome in the anaerobic protist Trichomonas vaginalis

P J Johnson et al. J Parasitol. 1993 Oct.

Abstract

Trichomonas vaginalis is a primitive protist that lacks mitochondria and peroxisomes. This aerotolerant anaerobe does, however, contain a specialized organelle involved in carbohydrate metabolism called the hydrogenosome. Hydrogenosomes are the site of fermentative oxidation of pyruvate, coupled to ATP production via substrate level phosphorylation. The organelle is surrounded by 2 membranes and appears to contain no genetic material. Hydrogenosomes are proposed to have arisen either through the conversion of mitochondria or via endosymbiosis with an anaerobic bacterium. Our studies show that hydrogenosomal proteins are synthesized on free polyribosomes and are, thus, posttranslationally translocated into the organelle. The 2 hydrogenosomal proteins we have examined in detail, ferredoxin and the beta subunit of succinyl CoA synthetase, appear to be synthesized as larger precursors that contain an 8- or 9-amino acid amino-terminal extension, respectively. These apparent leader sequences are absent from the mature proteins found in hydrogenosomes. The biochemical properties of the amino-terminal extensions are similar to one another and to mitochondrial presequences. These observations are consistent with the hypotheses that the specificity of protein translocation into hydrogenosomes is conferred by a short amino-terminal signal sequence and that the mechanisms underlying translocation are similar to that of mitochondria. Using in vitro import assays, we have shown that this short leader sequence is absolutely required for association of hydrogenosomal proteins with the organelle and that this association is dependent on ATP, temperature, and the presence of intact organelles.

PubMed Disclaimer

Cited by

Unusual Cell Structures and Organelles in Giardia intestinalis and Trichomonas vaginalis Are Potential Drug Targets.
Benchimol M, Gadelha AP, de Souza W. Benchimol M, et al. Microorganisms. 2022 Nov 2;10(11):2176. doi: 10.3390/microorganisms10112176. Microorganisms. 2022. PMID: 36363768 Free PMC article. Review.
The Trichomonas vaginalis hydrogenosome proteome is highly reduced relative to mitochondria, yet complex compared with mitosomes.
Schneider RE, Brown MT, Shiflett AM, Dyall SD, Hayes RD, Xie Y, Loo JA, Johnson PJ. Schneider RE, et al. Int J Parasitol. 2011 Nov;41(13-14):1421-34. doi: 10.1016/j.ijpara.2011.10.001. Epub 2011 Nov 9. Int J Parasitol. 2011. PMID: 22079833 Free PMC article.
Mitochondrion-related organelles in eukaryotic protists.
Shiflett AM, Johnson PJ. Shiflett AM, et al. Annu Rev Microbiol. 2010;64:409-29. doi: 10.1146/annurev.micro.62.081307.162826. Annu Rev Microbiol. 2010. PMID: 20528687 Free PMC article. Review.
A proteome reference map of Trichomonas vaginalis.
Huang KY, Chien KY, Lin YC, Hsu WM, Fong IK, Huang PJ, Yueh YM, Gan RR, Tang P. Huang KY, et al. Parasitol Res. 2009 Mar;104(4):927-33. doi: 10.1007/s00436-008-1274-z. Epub 2008 Dec 5. Parasitol Res. 2009. PMID: 19066965
Cardiolipin in hydrogenosomes: evidence of symbiotic origin.
de Andrade Rosa I, Einicker-Lamas M, Roney Bernardo R, Previatto LM, Mohana-Borges R, Morgado-Díaz JA, Benchimol M. de Andrade Rosa I, et al. Eukaryot Cell. 2006 Apr;5(4):784-7. doi: 10.1128/EC.5.4.784-787.2006. Eukaryot Cell. 2006. PMID: 16607026 Free PMC article.

Biogenesis of the hydrogenosome in the anaerobic protist Trichomonas vaginalis - PubMed (original) (raw)