Docking of acetyl-CoA carboxylase to the plastid envelope membrane attenuates fatty acid production in plants.
Nat Commun
; 11(1): 6191, 2020 12 03.
Article
en En
| MEDLINE
| ID: mdl-33273474
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.
Texto completo:
1
Base de datos:
MEDLINE
Asunto principal:
Acetil-CoA Carboxilasa
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Arabidopsis
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Ácidos Grasos
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Membranas Intracelulares
Idioma:
En
Revista:
Nat Commun
Asunto de la revista:
BIOLOGIA
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CIENCIA
Año:
2020
Tipo del documento:
Article