Evolution of the ferric reductase domain (FRD) superfamily: modularity, functional diversification, and signature motifs.

A heme-containing transmembrane ferric reductase domain (FRD) is found in bacterial and eukaryotic protein families, including ferric reductases (FRE), and NADPH oxidases (NOX). The aim of this study was to understand the phylogeny of the FRD superfamily. Bacteria contain FRD proteins consisting onl...

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Autores principales:	Xuezhi Zhang, Karl-Heinz Krause, Ioannis Xenarios, Thierry Soldati, Brigitte Boeckmann
Formato:	article
Lenguaje:	EN
Publicado:	Public Library of Science (PLoS) 2013
Materias:	Medicine R Science Q
Acceso en línea:	https://doaj.org/article/702887fcb9304a759e3b1b9810441ed4
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spelling	oai:doaj.org-article:702887fcb9304a759e3b1b9810441ed42021-11-18T07:54:24ZEvolution of the ferric reductase domain (FRD) superfamily: modularity, functional diversification, and signature motifs.1932-620310.1371/journal.pone.0058126https://doaj.org/article/702887fcb9304a759e3b1b9810441ed42013-01-01T00:00:00Zhttps://www.ncbi.nlm.nih.gov/pmc/articles/pmid/23505460/?tool=EBIhttps://doaj.org/toc/1932-6203A heme-containing transmembrane ferric reductase domain (FRD) is found in bacterial and eukaryotic protein families, including ferric reductases (FRE), and NADPH oxidases (NOX). The aim of this study was to understand the phylogeny of the FRD superfamily. Bacteria contain FRD proteins consisting only of the ferric reductase domain, such as YedZ and short bFRE proteins. Full length FRE and NOX enzymes are mostly found in eukaryotic cells and all possess a dehydrogenase domain, allowing them to catalyze electron transfer from cytosolic NADPH to extracellular metal ions (FRE) or oxygen (NOX). Metazoa possess YedZ-related STEAP proteins, possibly derived from bacteria through horizontal gene transfer. Phylogenetic analyses suggests that FRE enzymes appeared early in evolution, followed by a transition towards EF-hand containing NOX enzymes (NOX5- and DUOX-like). An ancestral gene of the NOX(1-4) family probably lost the EF-hands and new regulatory mechanisms of increasing complexity evolved in this clade. Two signature motifs were identified: NOX enzymes are distinguished from FRE enzymes through a four amino acid motif spanning from transmembrane domain 3 (TM3) to TM4, and YedZ/STEAP proteins are identified by the replacement of the first canonical heme-spanning histidine by a highly conserved arginine. The FRD superfamily most likely originated in bacteria.Xuezhi ZhangKarl-Heinz KrauseIoannis XenariosThierry SoldatiBrigitte BoeckmannPublic Library of Science (PLoS)articleMedicineRScienceQENPLoS ONE, Vol 8, Iss 3, p e58126 (2013)
institution	DOAJ
collection	DOAJ
language	EN
topic	Medicine R Science Q
spellingShingle	Medicine R Science Q Xuezhi Zhang Karl-Heinz Krause Ioannis Xenarios Thierry Soldati Brigitte Boeckmann Evolution of the ferric reductase domain (FRD) superfamily: modularity, functional diversification, and signature motifs.
description	A heme-containing transmembrane ferric reductase domain (FRD) is found in bacterial and eukaryotic protein families, including ferric reductases (FRE), and NADPH oxidases (NOX). The aim of this study was to understand the phylogeny of the FRD superfamily. Bacteria contain FRD proteins consisting only of the ferric reductase domain, such as YedZ and short bFRE proteins. Full length FRE and NOX enzymes are mostly found in eukaryotic cells and all possess a dehydrogenase domain, allowing them to catalyze electron transfer from cytosolic NADPH to extracellular metal ions (FRE) or oxygen (NOX). Metazoa possess YedZ-related STEAP proteins, possibly derived from bacteria through horizontal gene transfer. Phylogenetic analyses suggests that FRE enzymes appeared early in evolution, followed by a transition towards EF-hand containing NOX enzymes (NOX5- and DUOX-like). An ancestral gene of the NOX(1-4) family probably lost the EF-hands and new regulatory mechanisms of increasing complexity evolved in this clade. Two signature motifs were identified: NOX enzymes are distinguished from FRE enzymes through a four amino acid motif spanning from transmembrane domain 3 (TM3) to TM4, and YedZ/STEAP proteins are identified by the replacement of the first canonical heme-spanning histidine by a highly conserved arginine. The FRD superfamily most likely originated in bacteria.
format	article
author	Xuezhi Zhang Karl-Heinz Krause Ioannis Xenarios Thierry Soldati Brigitte Boeckmann
author_facet	Xuezhi Zhang Karl-Heinz Krause Ioannis Xenarios Thierry Soldati Brigitte Boeckmann
author_sort	Xuezhi Zhang
title	Evolution of the ferric reductase domain (FRD) superfamily: modularity, functional diversification, and signature motifs.
title_short	Evolution of the ferric reductase domain (FRD) superfamily: modularity, functional diversification, and signature motifs.
title_full	Evolution of the ferric reductase domain (FRD) superfamily: modularity, functional diversification, and signature motifs.
title_fullStr	Evolution of the ferric reductase domain (FRD) superfamily: modularity, functional diversification, and signature motifs.
title_full_unstemmed	Evolution of the ferric reductase domain (FRD) superfamily: modularity, functional diversification, and signature motifs.
title_sort	evolution of the ferric reductase domain (frd) superfamily: modularity, functional diversification, and signature motifs.
publisher	Public Library of Science (PLoS)
publishDate	2013
url	https://doaj.org/article/702887fcb9304a759e3b1b9810441ed4
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Evolution of the ferric reductase domain (FRD) superfamily: modularity, functional diversification, and signature motifs.

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