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

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...

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Autores principales: Richtová, Jitka, Sheiner, Lilach, Gruber, Ansgar, Yang, Shun-Min, Kořený, Luděk, Striepen, Boris, Oborník, Miroslav
Formato: Online Artículo Texto
Lenguaje:English
Publicado: MDPI 2021
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8233740/
https://www.ncbi.nlm.nih.gov/pubmed/34204357
http://dx.doi.org/10.3390/ijms22126495
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author Richtová, Jitka
Sheiner, Lilach
Gruber, Ansgar
Yang, Shun-Min
Kořený, Luděk
Striepen, Boris
Oborník, Miroslav
author_facet Richtová, Jitka
Sheiner, Lilach
Gruber, Ansgar
Yang, Shun-Min
Kořený, Luděk
Striepen, Boris
Oborník, Miroslav
author_sort Richtová, Jitka
collection PubMed
description 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.
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spelling pubmed-82337402021-06-27 Using Diatom and Apicomplexan Models to Study the Heme Pathway of Chromera velia Richtová, Jitka Sheiner, Lilach Gruber, Ansgar Yang, Shun-Min Kořený, Luděk Striepen, Boris Oborník, Miroslav Int J Mol Sci Article 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. MDPI 2021-06-17 /pmc/articles/PMC8233740/ /pubmed/34204357 http://dx.doi.org/10.3390/ijms22126495 Text en © 2021 by the authors. https://creativecommons.org/licenses/by/4.0/Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license (https://creativecommons.org/licenses/by/4.0/).
spellingShingle Article
Richtová, Jitka
Sheiner, Lilach
Gruber, Ansgar
Yang, Shun-Min
Kořený, Luděk
Striepen, Boris
Oborník, Miroslav
Using Diatom and Apicomplexan Models to Study the Heme Pathway of Chromera velia
title Using Diatom and Apicomplexan Models to Study the Heme Pathway of Chromera velia
title_full Using Diatom and Apicomplexan Models to Study the Heme Pathway of Chromera velia
title_fullStr Using Diatom and Apicomplexan Models to Study the Heme Pathway of Chromera velia
title_full_unstemmed Using Diatom and Apicomplexan Models to Study the Heme Pathway of Chromera velia
title_short Using Diatom and Apicomplexan Models to Study the Heme Pathway of Chromera velia
title_sort using diatom and apicomplexan models to study the heme pathway of chromera velia
topic Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8233740/
https://www.ncbi.nlm.nih.gov/pubmed/34204357
http://dx.doi.org/10.3390/ijms22126495
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