Using diatom and apicomplexan models to study the heme pathway of Chromera velia

Richtová, J., Sheiner, L. , Gruber, A., Yang, S.-M., Kořený, L., Striepen, B. and Oborník, M. (2021) Using diatom and apicomplexan models to study the heme pathway of Chromera velia. International Journal of Molecular Sciences, 22(12), 6495. (doi: 10.3390/ijms22126495) (PMID:34204357) (PMCID:PMC8233740)

Abstract

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.

• Item Type: Articles
• Additional Information: This research was funded by Czech Science Foundation, grant number 21-03224S and ERDF/ESF, Centre for Research of Pathogenicity and Virulence of Parasites, grant number CZ.02.1.01/0.0/0.0/16_019/0000759.
• Keywords: Tetrapyrrole biosynthesis, heterologous expression, Chromera velia, predictions.
• Status: Published
• Refereed: Yes
• Glasgow Author(s) Enlighten ID: Sheiner, Professor Lilach

Creator Roles

Sheiner, L.: Conceptualization, Methodology, Validation, Investigation, Resources, Writing – review and editing, Supervision

• Authors: Richtová, J., Sheiner, L., Gruber, A., Yang, S.-M., Kořený, L., Striepen, B., and Oborník, M.
• College/School: College of Medical Veterinary and Life Sciences > School of Infection & Immunity
• Journal Name: International Journal of Molecular Sciences
• Publisher: MDPI
• ISSN: 1661-6596
• ISSN (Online): 1422-0067
• Published Online: 17 June 2021
• Copyright Holders: Copyright © 2021 The Authors
• First Published: First published in International Journal of Molecular Sciences 22(12): 6495
• Publisher Policy: Reproduced under a Creative Commons License