Iron-sulfur protein NFU2 is required for branched-chain amino acid synthesis in Arabidopsis roots

Bibliographische Detailangaben
Veröffentlicht in:	Journal of experimental botany. - 1985. - 70(2019), 6 vom: 27. März, Seite 1875-1889
1. Verfasser:	Touraine, Brigitte (VerfasserIn)
Weitere Verfasser:	Vignols, Florence, Przybyla-Toscano, Jonathan, Ischebeck, Till, Dhalleine, Tiphaine, Wu, Hui-Chen, Magno, Cyril, Berger, Nathalie, Couturier, Jérémy, Dubos, Christian, Feussner, Ivo, Caffarri, Stefano, Havaux, Michel, Rouhier, Nicolas, Gaymard, Frédéric
Format:	Online-Aufsatz
Sprache:	English
Veröffentlicht:	2019
Zugriff auf das übergeordnete Werk:	Journal of experimental botany
Schlagworte:	Journal Article Research Support, Non-U.S. Gov't Arabidopsis thaliana branched-chain amino acids chloroplast development iron–sulfur protein photosynthesis AT4G01940 protein, Arabidopsis Amino Acids, Branched-Chain mehr... Arabidopsis Proteins Chloroplast Proteins Iron-Sulfur Proteins NFU3 protein, Arabidopsis Nfu2 protein, Arabidopsis

Beschreibung
Zusammenfassung:	© The Author(s) 2019. Published by Oxford University Press on behalf of the Society for Experimental Biology. All rights reserved. For permissions, please email: journals.permissionsoup.com. Numerous proteins require a metallic co-factor for their function. In plastids, the maturation of iron-sulfur (Fe-S) proteins necessitates a complex assembly machinery. In this study, we focused on Arabidopsis thaliana NFU1, NFU2, and NFU3, which participate in the final steps of the maturation process. According to the strong photosynthetic defects observed in high chlorophyll fluorescence 101 (hcf101), nfu2, and nfu3 plants, we determined that NFU2 and NFU3, but not NFU1, act immediately upstream of HCF101 for the maturation of [Fe4S4]-containing photosystem I subunits. An additional function of NFU2 in the maturation of the [Fe2S2] cluster of a dihydroxyacid dehydratase was obvious from the accumulation of precursors of the branched-chain amino acid synthesis pathway in roots of nfu2 plants and from the rescue of the primary root growth defect by supplying branched-chain amino acids. The absence of NFU3 in roots precluded any compensation. Overall, unlike their eukaryotic and prokaryotic counterparts, which are specific to [Fe4S4] proteins, NFU2 and NFU3 contribute to the maturation of both [Fe2S2] and [Fe4S4] proteins, either as a relay in conjunction with other proteins such as HCF101 or by directly delivering Fe-S clusters to client proteins. Considering the low number of Fe-S cluster transfer proteins relative to final acceptors, additional targets probably await identification
Beschreibung:	Date Completed 26.05.2020 Date Revised 25.08.2020 published: Print Citation Status MEDLINE
ISSN:	1460-2431
DOI:	10.1093/jxb/erz050