Docking of acetyl-CoA carboxylase to the plastid envelope membrane attenuates fatty acid production in plants

Autor: Ye, Yajin, Nikovics, Krisztina, To, Alexandra, Lepiniec, Loïc, Fedosejevs, Eric T., Van Doren, Steven R., Baud, Sébastien, Thelen, Jay J.
Přispěvatelé: University of Missouri [Columbia] (Mizzou), University of Missouri System, Institut Jean-Pierre Bourgin (IJPB), AgroParisTech-Université Paris-Saclay-Institut National de Recherche pour l’Agriculture, l’Alimentation et l’Environnement (INRAE), National Science Foundation (grants MCB-1716688 and PGRP IOS-1829365, ANR-11-BTBR-0004,RAPSODYN,Optimisation de la teneur et du rendement en huile chez le colza cultivé sous contrainte azotée(2011), ANR-17-EURE-0007,SPS-GSR,Ecole Universitaire de Recherche de Sciences des Plantes de Paris-Saclay(2017)
Jazyk: angličtina
Rok vydání: 2020
Předmět:
Zdroj: Nature Communications
Nature Communications, Nature Publishing Group, 2020, 11 (1), ⟨10.1038/s41467-020-20014-5⟩
Nature Communications, Vol 11, Iss 1, Pp 1-14 (2020)
ISSN: 2041-1723
DOI: 10.1038/s41467-020-20014-5⟩
Popis: In plants, light-dependent activation of de novo fatty acid synthesis (FAS) is partially mediated by acetyl-CoA carboxylase (ACCase), the first committed step for this pathway. However, it is not fully understood how plants control light-dependent FAS regulation to meet the cellular demand for acyl chains. We report here the identification of a gene family encoding for three small plastidial proteins of the envelope membrane that interact with the α-carboxyltransferase (α-CT) subunit of ACCase and participate in an original mechanism restraining FAS in the light. Light enhances the interaction between carboxyltransferase interactors (CTIs) and α-CT, which in turn attenuates carbon flux into FAS. Knockouts for CTI exhibit higher rates of FAS and marked increase in absolute triacylglycerol levels in leaves, more than 4-fold higher than in wild-type plants. Furthermore, WRINKLED1, a master transcriptional regulator of FAS, positively regulates CTI1 expression by direct binding to its promoter. This study reveals that in addition to light-dependent activation, “envelope docking” of ACCase permits fine-tuning of fatty acid supply during the plant life cycle.
In plants, light-dependent activation fatty acid synthesis (FAS) is mediated in part by acetyl-CoA carboxylase (ACCase). Here the authors identify a family of genes encoding carboxyltransferase interactors that attenuate FAS in the light by docking acetyl-CoA carboxylase to the plastid envelope.
Databáze: OpenAIRE