Abstract
The elongation of very-long-chain fatty acids is a conserved process used for the production of many metabolites, including plant cuticular waxes. The elongation of precursors of the most abundant cuticular wax components of some plants, however, is unique in requiring ECERIFERUM2-LIKE (CER2-LIKE) proteins. CER2-LIKEs are a clade within the BAHD superfamily of acyltransferases. They are known to be required for cuticular wax production in both Arabidopsis and maize based on mutant studies. Heterologous expression of Arabidopsis and rice CER2-LIKEs in Saccharomyces cerevisiae has demonstrated that they modify the chain-length specificity of elongation when paired with particular condensing enzymes. Despite sequence homology, CER2-LIKEs are distinct from the BAHD superfamily in that they do not appear to use acyl transfer activity to fulfill their biological function. Here, we review the discovery and characterization of CER2-LIKEs, propose several models to explain their function, and explore the importance of CER2-LIKE proteins for the evolution of plant cuticles.
Highlights
The elongation of very-long-chain fatty acids is a conserved process used for the production of many metabolites, including plant cuticular waxes
Identification and characterization of Arabidopsis ECERIFERUM2-LIKEs (CER2-LIKEs) has revealed that proteins encoded by these genes play a key role in modifying the activity of specific condensing enzymes, and enable the production of very-long-chain fatty acids (VLCFAs) precursors of cuticular waxes longer than 28 carbons in length
CER6, a condensing enzyme known to have a central role in cuticular wax production in Arabidopsis [19], was previously reported to elongate VLCFAs only to 28 carbons when expressed in yeast cells
Summary
Lipid barriers are essential across all domains of life. For example, lipid bilayers serve as barriers that enable the organization and regulation of cellular processes. Identification and characterization of Arabidopsis ECERIFERUM2-LIKEs (CER2-LIKEs) has revealed that proteins encoded by these genes play a key role in modifying the activity of specific condensing enzymes, and enable the production of VLCFA precursors of cuticular waxes longer than 28 carbons in length. Given the current model of fatty acid elongation, it was not obvious why an acyltransferase would be required for elongation of particular chain lengths of acyl-CoAs. Because heterologous expression in yeast has been a useful tool for characterizing the core components of the plant fatty acid elongase, expression of CER2 in yeast was an obvious approach to decipher the role of this protein. CER6, a condensing enzyme known to have a central role in cuticular wax production in Arabidopsis [19], was previously reported to elongate VLCFAs only to 28 carbons when expressed in yeast cells. A null cer2-like mutant will certainly be required for further studies of this gene
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