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Using Diatom and Apicomplexan Models to Study the Heme Pathway of Chromera velia

Biology Centre CAS, Laboratory of Evolutionary Protistology, Institute of Parasitology, 370 05 České Budějovice, Czech Republic
Faculty of Science, University of South Bohemia, 370 05 České Budějovice, Czech Republic
Welcome Centre for Integrative Parasitology, College of Medical, Veterinary and Life Sciences, Institute of Infection, Immunity and Inflammation, University of Glasgow, Glasgow G12 8QQ, UK
Department of Biochemistry, University of Cambridge, Cambridge CB2 1TN, UK
Department of Pathobiology, School of Veterinary Medicine, University of Pennsylvania, Philadelphia, PA 19104, USA
Author to whom correspondence should be addressed.
Academic Editor: Bartolome Sabater
Int. J. Mol. Sci. 2021, 22(12), 6495;
Received: 17 May 2021 / Revised: 11 June 2021 / Accepted: 12 June 2021 / Published: 17 June 2021
(This article belongs to the Special Issue Chloroplast 3.0)
Heme biosynthesis is essential for almost all living organisms. Despite its conserved function, the pathway’s enzymes can be located in a remarkable diversity of cellular compartments in different organisms. This location does not always reflect their evolutionary origins, as might be expected from the history of their acquisition through endosymbiosis. Instead, the final subcellular localization of the enzyme reflects multiple factors, including evolutionary origin, demand for the product, availability of the substrate, and mechanism of pathway regulation. The biosynthesis of heme in the apicomonad Chromera velia follows a chimeric pathway combining heme elements from the ancient algal symbiont and the host. Computational analyses using different algorithms predict complex targeting patterns, placing enzymes in the mitochondrion, plastid, endoplasmic reticulum, or the cytoplasm. We employed heterologous reporter gene expression in the apicomplexan parasite Toxoplasma gondii and the diatom Phaeodactylum tricornutum to experimentally test these predictions. 5-aminolevulinate synthase was located in the mitochondria in both transfection systems. In T. gondii, the two 5-aminolevulinate dehydratases were located in the cytosol, uroporphyrinogen synthase in the mitochondrion, and the two ferrochelatases in the plastid. In P. tricornutum, all remaining enzymes, from ALA-dehydratase to ferrochelatase, were placed either in the endoplasmic reticulum or in the periplastidial space. View Full-Text
Keywords: tetrapyrrole biosynthesis; heterologous expression; Chromera velia; predictions tetrapyrrole biosynthesis; heterologous expression; Chromera velia; predictions
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MDPI and ACS Style

Richtová, J.; Sheiner, L.; Gruber, A.; Yang, S.-M.; Kořený, L.; Striepen, B.; Oborník, M. Using Diatom and Apicomplexan Models to Study the Heme Pathway of Chromera velia. Int. J. Mol. Sci. 2021, 22, 6495.

AMA Style

Richtová J, Sheiner L, Gruber A, Yang S-M, Kořený L, Striepen B, Oborník M. Using Diatom and Apicomplexan Models to Study the Heme Pathway of Chromera velia. International Journal of Molecular Sciences. 2021; 22(12):6495.

Chicago/Turabian Style

Richtová, Jitka, Lilach Sheiner, Ansgar Gruber, Shun-Min Yang, Luděk Kořený, Boris Striepen, and Miroslav Oborník. 2021. "Using Diatom and Apicomplexan Models to Study the Heme Pathway of Chromera velia" International Journal of Molecular Sciences 22, no. 12: 6495.

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