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In Campylobacter jejuni, a new type of chaperone receives heme from ferrochelatase
Intracellular heme formation and trafficking are fundamental processes in living organisms. Bacteria and archaea utilize three biogenesis pathways to produce iron protoporphyrin IX (heme b) that diverge after the formation of the common intermediate uroporphyrinogen III (uro’gen III). In this study,...
Autores principales: | , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Frontiers Media S.A.
2023
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC10320005/ https://www.ncbi.nlm.nih.gov/pubmed/37415606 http://dx.doi.org/10.3389/fgene.2023.1199357 |
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author | Zamarreño Beas, Jordi Videira, Marco A. M. Karavaeva, Val Lourenço, Frederico M. Almeida, Mafalda R. Sousa, Filipa Saraiva, Lígia M. |
author_facet | Zamarreño Beas, Jordi Videira, Marco A. M. Karavaeva, Val Lourenço, Frederico M. Almeida, Mafalda R. Sousa, Filipa Saraiva, Lígia M. |
author_sort | Zamarreño Beas, Jordi |
collection | PubMed |
description | Intracellular heme formation and trafficking are fundamental processes in living organisms. Bacteria and archaea utilize three biogenesis pathways to produce iron protoporphyrin IX (heme b) that diverge after the formation of the common intermediate uroporphyrinogen III (uro’gen III). In this study, we identify and provide a detailed characterization of the enzymes involved in the transformation of uro’gen III into heme in Campylobacter jejuni, demonstrating that this bacterium utilizes the protoporphyrin-dependent (PPD) pathway. In general, limited knowledge exists regarding the mechanisms by which heme b reaches its target proteins after this final step. Specifically, the chaperones necessary for trafficking heme to prevent the cytotoxic effects associated with free heme remain largely unidentified. In C. jejuni, we identified a protein named CgdH2 that binds heme with a dissociation constant of 4.9 ± 1.0 µM, and this binding is impaired upon mutation of residues histidine 45 and 133. We demonstrate that C. jejuni CgdH2 establishes protein–protein interactions with ferrochelatase, suggesting its role in facilitating heme transfer from ferrochelatase to CgdH2. Furthermore, phylogenetic analysis reveals that C. jejuni CgdH2 is evolutionarily distinct from the currently known chaperones. Therefore, CgdH2 is the first protein identified as an acceptor of intracellularly formed heme, expanding our knowledge of the mechanisms underlying heme trafficking within bacterial cells. |
format | Online Article Text |
id | pubmed-10320005 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2023 |
publisher | Frontiers Media S.A. |
record_format | MEDLINE/PubMed |
spelling | pubmed-103200052023-07-06 In Campylobacter jejuni, a new type of chaperone receives heme from ferrochelatase Zamarreño Beas, Jordi Videira, Marco A. M. Karavaeva, Val Lourenço, Frederico M. Almeida, Mafalda R. Sousa, Filipa Saraiva, Lígia M. Front Genet Genetics Intracellular heme formation and trafficking are fundamental processes in living organisms. Bacteria and archaea utilize three biogenesis pathways to produce iron protoporphyrin IX (heme b) that diverge after the formation of the common intermediate uroporphyrinogen III (uro’gen III). In this study, we identify and provide a detailed characterization of the enzymes involved in the transformation of uro’gen III into heme in Campylobacter jejuni, demonstrating that this bacterium utilizes the protoporphyrin-dependent (PPD) pathway. In general, limited knowledge exists regarding the mechanisms by which heme b reaches its target proteins after this final step. Specifically, the chaperones necessary for trafficking heme to prevent the cytotoxic effects associated with free heme remain largely unidentified. In C. jejuni, we identified a protein named CgdH2 that binds heme with a dissociation constant of 4.9 ± 1.0 µM, and this binding is impaired upon mutation of residues histidine 45 and 133. We demonstrate that C. jejuni CgdH2 establishes protein–protein interactions with ferrochelatase, suggesting its role in facilitating heme transfer from ferrochelatase to CgdH2. Furthermore, phylogenetic analysis reveals that C. jejuni CgdH2 is evolutionarily distinct from the currently known chaperones. Therefore, CgdH2 is the first protein identified as an acceptor of intracellularly formed heme, expanding our knowledge of the mechanisms underlying heme trafficking within bacterial cells. Frontiers Media S.A. 2023-06-21 /pmc/articles/PMC10320005/ /pubmed/37415606 http://dx.doi.org/10.3389/fgene.2023.1199357 Text en Copyright © 2023 Zamarreño Beas, Videira, Karavaeva, Lourenço, Almeida, Sousa and Saraiva. https://creativecommons.org/licenses/by/4.0/This is an open-access article distributed under the terms of the Creative Commons Attribution License (CC BY). The use, distribution or reproduction in other forums is permitted, provided the original author(s) and the copyright owner(s) are credited and that the original publication in this journal is cited, in accordance with accepted academic practice. No use, distribution or reproduction is permitted which does not comply with these terms. |
spellingShingle | Genetics Zamarreño Beas, Jordi Videira, Marco A. M. Karavaeva, Val Lourenço, Frederico M. Almeida, Mafalda R. Sousa, Filipa Saraiva, Lígia M. In Campylobacter jejuni, a new type of chaperone receives heme from ferrochelatase |
title | In Campylobacter jejuni, a new type of chaperone receives heme from ferrochelatase |
title_full | In Campylobacter jejuni, a new type of chaperone receives heme from ferrochelatase |
title_fullStr | In Campylobacter jejuni, a new type of chaperone receives heme from ferrochelatase |
title_full_unstemmed | In Campylobacter jejuni, a new type of chaperone receives heme from ferrochelatase |
title_short | In Campylobacter jejuni, a new type of chaperone receives heme from ferrochelatase |
title_sort | in campylobacter jejuni, a new type of chaperone receives heme from ferrochelatase |
topic | Genetics |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC10320005/ https://www.ncbi.nlm.nih.gov/pubmed/37415606 http://dx.doi.org/10.3389/fgene.2023.1199357 |
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