Nodule-specific Cu+ -chaperone NCC1 is required for symbiotic nitrogen fixation in Medicago truncatula root nodules

© 2023 The Authors New Phytologist © 2023 New Phytologist Foundation.

Bibliographische Detailangaben
Veröffentlicht in:The New phytologist. - 1979. - 241(2023), 2 vom: 01. Jan., Seite 793-810
1. Verfasser: Navarro-Gómez, Cristina (VerfasserIn)
Weitere Verfasser: León-Mediavilla, Javier, Küpper, Hendrik, Rodríguez-Simón, Mario, Paganelli-López, Alba, Wen, Jiangqi, Burén, Stefan, Mysore, Kirankumar S, Bokhari, Syed Nadeem Hussain, Imperial, Juan, Escudero, Viviana, González-Guerrero, Manuel
Format: Online-Aufsatz
Sprache:English
Veröffentlicht: 2024
Zugriff auf das übergeordnete Werk:The New phytologist
Schlagworte:Journal Article copper copper transport metallochaperone nitrogen fixation nodulation Copper 789U1901C5 Plant Proteins
Beschreibung
Zusammenfassung:© 2023 The Authors New Phytologist © 2023 New Phytologist Foundation.
Cu+ -chaperones are a diverse group of proteins that allocate Cu+ ions to specific copper proteins, creating different copper pools targeted to specific physiological processes. Symbiotic nitrogen fixation carried out in legume root nodules indirectly requires relatively large amounts of copper, for example for energy delivery via respiration, for which targeted copper deliver systems would be required. MtNCC1 is a nodule-specific Cu+ -chaperone encoded in the Medicago truncatula genome, with a N-terminus Atx1-like domain that can bind Cu+ with picomolar affinities. MtNCC1 is able to interact with nodule-specific Cu+ -importer MtCOPT1. MtNCC1 is expressed primarily from the late infection zone to the early fixation zone and is located in the cytosol, associated with plasma and symbiosome membranes, and within nuclei. Consistent with its key role in nitrogen fixation, ncc1 mutants have a severe reduction in nitrogenase activity and a 50% reduction in copper-dependent cytochrome c oxidase activity. A subset of the copper proteome is also affected in the ncc1 mutant nodules. Many of these proteins can be pulled down when using a Cu+ -loaded N-terminal MtNCC1 moiety as a bait, indicating a role in nodule copper homeostasis and in copper-dependent physiological processes. Overall, these data suggest a pleiotropic role of MtNCC1 in copper delivery for symbiotic nitrogen fixation
Beschreibung:Date Completed 22.12.2023
Date Revised 22.12.2023
published: Print-Electronic
Citation Status MEDLINE
ISSN:1469-8137
DOI:10.1111/nph.19360