Mitochondrial complex I dysfunction increases CO2 efflux and reconfigures metabolic fluxes of day respiration in tobacco leaves

© 2018 The Authors. New Phytologist © 2018 New Phytologist Trust.

Bibliographische Detailangaben
Veröffentlicht in:The New phytologist. - 1979. - 221(2019), 2 vom: 01. Jan., Seite 750-763
1. Verfasser: Lothier, Jérémy (VerfasserIn)
Weitere Verfasser: De Paepe, Rosine, Tcherkez, Guillaume
Format: Online-Aufsatz
Sprache:English
Veröffentlicht: 2019
Zugriff auf das übergeordnete Werk:The New phytologist
Schlagworte:Journal Article Research Support, Non-U.S. Gov't CO2 efflux day respiration (Rd) isotopic labeling photorespiration tricarboxylic acid cycle Carbon Isotopes Gases Carbon Dioxide mehr... 142M471B3J Pyruvic Acid 8558G7RUTR Electron Transport Complex I EC 7.1.1.2 Carbon-13 FDJ0A8596D
Beschreibung
Zusammenfassung:© 2018 The Authors. New Phytologist © 2018 New Phytologist Trust.
Mutants affected in complex I are useful to understand the role played by mitochondrial electron transport and redox metabolism in cellular homeostasis and signaling. However, their respiratory phenotype is incompletely described and a specific examination of day respiration (Rd ) is lacking. Here, we used isotopic methods and metabolomics to investigate the impact of complex I dysfunction on Rd in two respiratory mutants of forest tobacco (Nicotiana sylvestris): cytoplasmic male sterile II (CMSII) and nuclear male sterile 1 (NMS1), previously characterized for complex I disruption. Rd was higher in mutants and the inhibition of leaf respiration by light was lower. Higher Rd values were caused by increased (phosphoenol)pyruvate (PEP) metabolism at the expense of anaplerotic (PEP carboxylase (PEPc) -catalyzed) activity. De novo synthesis of Krebs cycle intermediates in the light was larger in mutants than in the wild-type, although numerically small in all genotypes. Carbon metabolism in mutants involved alternative pathways, such as alanine synthesis, and an increase in amino acid production with the notable exception of aspartate. Our results show that the alteration of NADH re-oxidation activity by complex I does not cause a general inhibition of catabolism, but rather a re-orchestration of fluxes in day respiratory metabolism, leading to an increased CO2 efflux
Beschreibung:Date Completed 14.01.2020
Date Revised 13.12.2023
published: Print-Electronic
Citation Status MEDLINE
ISSN:1469-8137
DOI:10.1111/nph.15393