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

0554920 - BC 2022 RIV CH eng J - Článek v odborném periodiku
Richtová, Jitka - Sheiner, L. - Gruber, Ansgar - Yang, Shun-Min - Kořený, L. - Striepen, B. - Oborník, Miroslav
Using Diatom and Apicomplexan Models to Study the Heme Pathway of Chromera velia.
International Journal of Molecular Sciences. Roč. 22, č. 12 (2021), č. článku 6495. E-ISSN 1422-0067
Grant CEP: GA ČR(CZ) GA21-03224S; GA MŠMT(CZ) EF16_019/0000759
Institucionální podpora: RVO:60077344
Klíčová slova: toxoplasma-gondii * protein import * tetrapyrrole biosynthesis * phaeodactylum-tricornutum * nuclear transformation * plasmodium-falciparum * targeting sequences * secondary plastids * ferrochelatase * trafficking * tetrapyrrole biosynthesis * heterologous expression * Chromera velia * predictions
Obor OECD: Biology (theoretical, mathematical, thermal, cryobiology, biological rhythm), Evolutionary biology
Impakt faktor: 6.208, rok: 2021
Způsob publikování: Open access
https://pubmed.ncbi.nlm.nih.gov/34204357/

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.
Trvalý link: http://hdl.handle.net/11104/0329557