<named-content content-type="genus-species">Chlamydomonas reinhardtii</named-content> LFO1 Is an IsdG Family Heme Oxygenase

ABSTRACT Heme is essential for respiration across all domains of life. However, heme accumulation can lead to toxicity if cells are unable to either degrade or export heme or its toxic by-products. Under aerobic conditions, heme degradation is performed by heme oxygenases, enzymes which utilize oxyg...

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Autores principales:	Lisa J. Lojek, Allison J. Farrand, Jennifer H. Wisecaver, Crysten E. Blaby-Haas, Brian W. Michel, Sabeeha S. Merchant, Antonis Rokas, Eric P. Skaar
Formato:	article
Lenguaje:	EN
Publicado:	American Society for Microbiology 2017
Materias:	Chlamydomonas bilin heme heme degradatrion iron monooxygenases Microbiology QR1-502
Acceso en línea:	https://doaj.org/article/e779373f48724f7fbad545b38962453b
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spelling	oai:doaj.org-article:e779373f48724f7fbad545b38962453b2021-11-15T15:22:05Z<named-content content-type="genus-species">Chlamydomonas reinhardtii</named-content> LFO1 Is an IsdG Family Heme Oxygenase10.1128/mSphere.00176-172379-5042https://doaj.org/article/e779373f48724f7fbad545b38962453b2017-08-01T00:00:00Zhttps://journals.asm.org/doi/10.1128/mSphere.00176-17https://doaj.org/toc/2379-5042ABSTRACT Heme is essential for respiration across all domains of life. However, heme accumulation can lead to toxicity if cells are unable to either degrade or export heme or its toxic by-products. Under aerobic conditions, heme degradation is performed by heme oxygenases, enzymes which utilize oxygen to cleave the tetrapyrrole ring of heme. The HO-1 family of heme oxygenases has been identified in both bacterial and eukaryotic cells, whereas the IsdG family has thus far been described only in bacteria. We identified a hypothetical protein in the eukaryotic green alga Chlamydomonas reinhardtii, which encodes a protein containing an antibiotic biosynthesis monooxygenase (ABM) domain consistent with those associated with IsdG family members. This protein, which we have named LFO1, degrades heme, contains similarities in predicted secondary structures to IsdG family members, and retains the functionally conserved catalytic residues found in all IsdG family heme oxygenases. These data establish LFO1 as an IsdG family member and extend our knowledge of the distribution of IsdG family members beyond bacteria. To gain further insight into the distribution of the IsdG family, we used the LFO1 sequence to identify 866 IsdG family members, including representatives from all domains of life. These results indicate that the distribution of IsdG family heme oxygenases is more expansive than previously appreciated, underscoring the broad relevance of this enzyme family. IMPORTANCE This work establishes a protein in the freshwater alga Chlamydomonas reinhardtii as an IsdG family heme oxygenase. This protein, LFO1, exhibits predicted secondary structure and catalytic residues conserved in IsdG family members, in addition to a chloroplast localization sequence. Additionally, the catabolite that results from the degradation of heme by LFO1 is distinct from that of other heme degradation products. Using LFO1 as a seed, we performed phylogenetic analysis, revealing that the IsdG family is conserved in all domains of life. Additionally, C. reinhardtii contains two previously identified HO-1 family heme oxygenases, making C. reinhardtii the first organism shown to contain two families of heme oxygenases. These data indicate that C. reinhardtii may have unique mechanisms for regulating iron homeostasis within the chloroplast.Lisa J. LojekAllison J. FarrandJennifer H. WisecaverCrysten E. Blaby-HaasBrian W. MichelSabeeha S. MerchantAntonis RokasEric P. SkaarAmerican Society for MicrobiologyarticleChlamydomonasbilinhemeheme degradatrionironmonooxygenasesMicrobiologyQR1-502ENmSphere, Vol 2, Iss 4 (2017)
institution	DOAJ
collection	DOAJ
language	EN
topic	Chlamydomonas bilin heme heme degradatrion iron monooxygenases Microbiology QR1-502
spellingShingle	Chlamydomonas bilin heme heme degradatrion iron monooxygenases Microbiology QR1-502 Lisa J. Lojek Allison J. Farrand Jennifer H. Wisecaver Crysten E. Blaby-Haas Brian W. Michel Sabeeha S. Merchant Antonis Rokas Eric P. Skaar <named-content content-type="genus-species">Chlamydomonas reinhardtii</named-content> LFO1 Is an IsdG Family Heme Oxygenase
description	ABSTRACT Heme is essential for respiration across all domains of life. However, heme accumulation can lead to toxicity if cells are unable to either degrade or export heme or its toxic by-products. Under aerobic conditions, heme degradation is performed by heme oxygenases, enzymes which utilize oxygen to cleave the tetrapyrrole ring of heme. The HO-1 family of heme oxygenases has been identified in both bacterial and eukaryotic cells, whereas the IsdG family has thus far been described only in bacteria. We identified a hypothetical protein in the eukaryotic green alga Chlamydomonas reinhardtii, which encodes a protein containing an antibiotic biosynthesis monooxygenase (ABM) domain consistent with those associated with IsdG family members. This protein, which we have named LFO1, degrades heme, contains similarities in predicted secondary structures to IsdG family members, and retains the functionally conserved catalytic residues found in all IsdG family heme oxygenases. These data establish LFO1 as an IsdG family member and extend our knowledge of the distribution of IsdG family members beyond bacteria. To gain further insight into the distribution of the IsdG family, we used the LFO1 sequence to identify 866 IsdG family members, including representatives from all domains of life. These results indicate that the distribution of IsdG family heme oxygenases is more expansive than previously appreciated, underscoring the broad relevance of this enzyme family. IMPORTANCE This work establishes a protein in the freshwater alga Chlamydomonas reinhardtii as an IsdG family heme oxygenase. This protein, LFO1, exhibits predicted secondary structure and catalytic residues conserved in IsdG family members, in addition to a chloroplast localization sequence. Additionally, the catabolite that results from the degradation of heme by LFO1 is distinct from that of other heme degradation products. Using LFO1 as a seed, we performed phylogenetic analysis, revealing that the IsdG family is conserved in all domains of life. Additionally, C. reinhardtii contains two previously identified HO-1 family heme oxygenases, making C. reinhardtii the first organism shown to contain two families of heme oxygenases. These data indicate that C. reinhardtii may have unique mechanisms for regulating iron homeostasis within the chloroplast.
format	article
author	Lisa J. Lojek Allison J. Farrand Jennifer H. Wisecaver Crysten E. Blaby-Haas Brian W. Michel Sabeeha S. Merchant Antonis Rokas Eric P. Skaar
author_facet	Lisa J. Lojek Allison J. Farrand Jennifer H. Wisecaver Crysten E. Blaby-Haas Brian W. Michel Sabeeha S. Merchant Antonis Rokas Eric P. Skaar
author_sort	Lisa J. Lojek
title	<named-content content-type="genus-species">Chlamydomonas reinhardtii</named-content> LFO1 Is an IsdG Family Heme Oxygenase
title_short	<named-content content-type="genus-species">Chlamydomonas reinhardtii</named-content> LFO1 Is an IsdG Family Heme Oxygenase
title_full	<named-content content-type="genus-species">Chlamydomonas reinhardtii</named-content> LFO1 Is an IsdG Family Heme Oxygenase
title_fullStr	<named-content content-type="genus-species">Chlamydomonas reinhardtii</named-content> LFO1 Is an IsdG Family Heme Oxygenase
title_full_unstemmed	<named-content content-type="genus-species">Chlamydomonas reinhardtii</named-content> LFO1 Is an IsdG Family Heme Oxygenase
title_sort	<named-content content-type="genus-species">chlamydomonas reinhardtii</named-content> lfo1 is an isdg family heme oxygenase
publisher	American Society for Microbiology
publishDate	2017
url	https://doaj.org/article/e779373f48724f7fbad545b38962453b
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<named-content content-type="genus-species">Chlamydomonas reinhardtii</named-content> LFO1 Is an IsdG Family Heme Oxygenase

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