Evolutionary and structural analyses of the NADPH oxidase family in eukaryotes reveal an initial calcium dependency.


Journal

Redox biology
ISSN: 2213-2317
Titre abrégé: Redox Biol
Pays: Netherlands
ID NLM: 101605639

Informations de publication

Date de publication:
10 2022
Historique:
received: 01 07 2022
revised: 04 08 2022
accepted: 08 08 2022
pubmed: 24 8 2022
medline: 28 9 2022
entrez: 23 8 2022
Statut: ppublish

Résumé

Reactive oxygen species are unstable molecules generated by the partial reduction of dioxygen. NADPH oxidases are a ubiquitous family of enzymes devoted to ROS production. They fuel an array of physiological roles in different species and are chemically demanding enzymes requiring FAD, NADPH and heme prosthetic groups in addition to either calcium or a various number of cytosolic mediators for activity. These activating partners are exclusive components that partition and distinguish the NOX members from one another. To gain insight into the evolution of these activating mechanisms, and in general in their evolutionary history, we conducted an in-depth phylogenetic analysis of the NADPH oxidase family in eukaryotes. We show that all characterized NOXs share a common ancestor, which comprised a fully formed catalytic unit. Regarding the activation mode, we identified calcium-dependency as the earliest form of NOX regulation. The protein-protein mode of regulation would have evolved more recently by gene-duplication with the concomitant loss of the EF-hands motif region. These more recent events generated the diversely activated NOX systems as observed in extant animals and fungi.

Identifiants

pubmed: 35998431
pii: S2213-2317(22)00208-7
doi: 10.1016/j.redox.2022.102436
pmc: PMC9421330
pii:
doi:

Substances chimiques

Reactive Oxygen Species 0
Flavin-Adenine Dinucleotide 146-14-5
Heme 42VZT0U6YR
NADP 53-59-8
NADPH Oxidase 1 EC 1.6.3.-
NADPH Oxidase 4 EC 1.6.3.-
NADPH Oxidases EC 1.6.3.-
Oxygen S88TT14065
Calcium SY7Q814VUP

Types de publication

Journal Article Research Support, Non-U.S. Gov't

Langues

eng

Sous-ensembles de citation

IM

Pagination

102436

Informations de copyright

Copyright © 2022 The Authors. Published by Elsevier B.V. All rights reserved.

Déclaration de conflit d'intérêts

Declaration of competing interest The Authors declare no conflicts of interest.

Auteurs

Marta Massari (M)

Department of Biology and Biotechnology Lazzaro Spallanzani, University of Pavia, Via Ferrata 9, 27100, Pavia, Italy.

Callum R Nicoll (CR)

Department of Biology and Biotechnology Lazzaro Spallanzani, University of Pavia, Via Ferrata 9, 27100, Pavia, Italy.

Sara Marchese (S)

Department of Biology and Biotechnology Lazzaro Spallanzani, University of Pavia, Via Ferrata 9, 27100, Pavia, Italy.

Andrea Mattevi (A)

Department of Biology and Biotechnology Lazzaro Spallanzani, University of Pavia, Via Ferrata 9, 27100, Pavia, Italy. Electronic address: andrea.mattevi@unipv.it.

Maria Laura Mascotti (ML)

Molecular Enzymology, Groningen Biomolecular Sciences and Biotechnology Institute, University of Groningen, Nijenborgh 4, 9747, AG Groningen, the Netherlands; IMIBIO-SL CONICET, Facultad de Química Bioquímica y Farmacia, Universidad Nacional de San Luis, Ejercito de los Andes 950, D5700HHW, San Luis, Argentina. Electronic address: m.l.mascotti@rug.nl.

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Classifications MeSH