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

Yajin Ye, Krisztina Nikovics, Alexandra To, Loïc Lepiniec, Eric T. Fedosejevs, Steven R. Doren, Sébastien Baud and Jay J. Thelen ()
Additional contact information
Yajin Ye: University of Missouri-Columbia
Krisztina Nikovics: Université Paris-Saclay
Alexandra To: Université Paris-Saclay
Loïc Lepiniec: Université Paris-Saclay
Eric T. Fedosejevs: University of Missouri-Columbia
Steven R. Doren: University of Missouri-Columbia
Sébastien Baud: Université Paris-Saclay
Jay J. Thelen: University of Missouri-Columbia

Nature Communications, 2020, vol. 11, issue 1, 1-14

Abstract: Abstract 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.

Date: 2020
References: Add references at CitEc
Citations:

Downloads: (external link)
https://www.nature.com/articles/s41467-020-20014-5 Abstract (text/html)

Related works:
This item may be available elsewhere in EconPapers: Search for items with the same title.

Export reference: BibTeX RIS (EndNote, ProCite, RefMan) HTML/Text

Persistent link: https://EconPapers.repec.org/RePEc:nat:natcom:v:11:y:2020:i:1:d:10.1038_s41467-020-20014-5

Ordering information: This journal article can be ordered from
https://www.nature.com/ncomms/

DOI: 10.1038/s41467-020-20014-5

Access Statistics for this article

Nature Communications is currently edited by Nathalie Le Bot, Enda Bergin and Fiona Gillespie

More articles in Nature Communications from Nature
Bibliographic data for series maintained by Sonal Shukla () and Springer Nature Abstracting and Indexing ().