Research article - Peer-reviewed, 2016
Biochemical characteristics of AtFAR2, a fatty acid reductase from Arabidopsis thaliana that reduces fatty acyl-CoA and -ACP substrates into fatty alcohols
Doan, Thuy; Carlsson, Anders S.; Stymne, Sten; Hofvander, PerAbstract
Fatty alcohols and derivatives are important for proper deposition of a functional pollen wall. Mutations in specific genes encoding fatty acid reductases (FAR) responsible for fatty alcohol production cause abnormal development of pollen. A disrupted AtFAR2 (MS2) gene in Arabidopsis thaliana results in pollen developing an abnormal exine layer and a reduced fertility phenotype. AtFAR2 has been shown to be targeted to chloroplasts and in a purified form to be specific for acyl-ACP substrates. Here, we present data on the in vitro and in planta characterizations of AtFAR2 from A. thaliana and show that this enzyme has the ability to use both, C16:0-ACPand C16:0-CoA, as substrates to produce C16:0-alcohol. Our results further show that AtFAR2 is highly similar in properties and substrate specificity to AtFAR6 for which in vitro data has been published, and which is also a chloroplast localized enzyme. This suggests that although AtFAR2 is the major enzyme responsible for exine layer functionality, AtFAR6 might provide functional redundancy to AtFAR2.Keywords
Arabidopsis thaliana; chloroplast; fatty acyl-CoA/ACP reductase; fatty alcohol; fatty aldehydePublished in
Acta Biochimica Polonica2016, volume: 63, number: 3, pages: 565-570
Publisher: ACTA BIOCHIMICA POLONICA
Authors' information
Swedish University of Agricultural Sciences, Department of Plant Breeding
Doan, Thuy
Nong Lam University
Carlsson, Anders S. (Carlsson, Anders)
Swedish University of Agricultural Sciences, Department of Plant Breeding
Swedish University of Agricultural Sciences, Department of Plant Breeding
UKÄ Subject classification
Biochemistry and Molecular Biology
Publication Identifiers
DOI: https://doi.org/10.18388/abp.2016_1245
URI (permanent link to this page)
https://res.slu.se/id/publ/79637