Campus Units

Biochemistry, Biophysics and Molecular Biology, Roy J. Carver Department of, Center for Metabolic Biology, NSF Engineering Research Center for Biorenewable Chemicals

Document Type

Article

Publication Version

Published Version

Publication Date

6-2020

Journal or Book Title

Plant Physiology

Volume

183

First Page

517

Last Page

529

DOI

10.1104/pp.19.01564

Abstract

Plant fatty acid biosynthesis occurs in both plastids and mitochondria. Here, we report the identification and characterization of Arabidopsis (Arabidopsis thaliana) genes encoding three enzymes shared between the mitochondria- and plastid-localized type II fatty acid synthase systems (mtFAS and ptFAS, respectively). Two of these enzymes, β-ketoacyl-acyl carrier protein (ACP) reductase and enoyl-ACP reductase, catalyze two of the reactions that constitute the core four-reaction cycle of the FAS system, which iteratively elongates the acyl chain by two carbon atoms per cycle. The third enzyme, malonyl-coenzyme A:ACP transacylase, catalyzes the reaction that loads the mtFAS system with substrate by malonylating the phosphopantetheinyl cofactor of ACP. GFP fusion experiments revealed that the these enzymes localize to both chloroplasts and mitochondria. This localization was validated by characterization of mutant alleles, which were rescued by transgenes expressing enzyme variants that were retargeted only to plastids or only to mitochondria. The singular retargeting of these proteins to plastids rescued the embryo lethality associated with disruption of the essential ptFAS system, but these rescued plants displayed phenotypes typical of the lack of mtFAS function, including reduced lipoylation of the H subunit of the glycine decarboxylase complex, hyperaccumulation of glycine, and reduced growth. However, these latter traits were reversible in an elevated-CO2 atmosphere, which suppresses mtFAS-associated photorespiration-dependent chemotypes. Sharing enzymatic components between mtFAS and ptFAS systems constrains the evolution of these nonredundant fatty acid biosynthetic machineries.

Comments

This article is published as Guan, Xin, Yozo Okazaki, Rwisdom Zhang, Kazuki Saito, and Basil J. Nikolau. "Dual-localized enzymatic components constitute the fatty acid synthase systems in mitochondria and plastids." Plant physiology 183, no. 2 (2020): 517-529. doi:10.1104/pp.19.01564.

Creative Commons License

Creative Commons Attribution 4.0 International License
This work is licensed under a Creative Commons Attribution 4.0 International License.

Copyright Owner

American Society of Plant Biologists

Language

en

File Format

application/pdf

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