An article Docking of acetyl-CoA carboxylase to the plastid envelope membrane attenuates fatty acid production in plants WOS:000608522800010 published article about CARRIER PROTEIN; ARABIDOPSIS; SPINACH; LIGHT; BIOSYNTHESIS; WRINKLED1; COENZYME; PHOSPHORYLATION; ACCUMULATION; GENES in [Ye, Yajin; Fedosejevs, Eric T.; Van Doren, Steven R.; Thelen, Jay J.] Univ Missouri, Christopher S Bond Life Sci Ctr, Dept Biochem, 1201 E Rollins, Columbia, MO 65211 USA; [Nikovics, Krisztina; To, Alexandra; Lepiniec, Loic; Baud, Sebastien] Univ Paris Saclay, AgroParisTech, Inst Jean Pierre Bourgin, INRAE,CNRS, F-78000 Versailles, France in 2020.0, Cited 60.0. SDS of cas: 61-82-5. The Name is 1H-1,2,4-Triazol-5-amine. Through research, I have a further understanding and discovery of 61-82-5
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 alpha-carboxyltransferase (alpha-CT) subunit of ACCase and participate in an original mechanism restraining FAS in the light. Light enhances the interaction between carboxyltransferase interactors (CTIs) and alpha-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.
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Reference:
Article; Safari, Niloufar; Shirini, Farhad; Tajik, Hassan; Journal of Molecular Structure; vol. 1201; (2020);,
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