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

Détails

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Etat: Public
Version: de l'auteur
ID Serval
serval:BIB_D88C72718728
Type
Article: article d'un périodique ou d'un magazine.
Collection
Publications
Titre
Evolution of the ferric reductase domain (FRD) superfamily: modularity, functional diversification, and signature motifs.
Périodique
PLoS One
Auteur(s)
Zhang X., Krause K.H., Xenarios I., Soldati T., Boeckmann B.
ISSN
1932-6203 (Electronic)
ISSN-L
1932-6203
Statut éditorial
Publié
Date de publication
2013
Volume
8
Numéro
3
Pages
e58126
Langue
anglais
Résumé
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.
Pubmed
Web of science
Open Access
Oui
Création de la notice
30/05/2013 13:17
Dernière modification de la notice
20/08/2019 15:58
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