LPEATs Tailor Plant Phospholipid Composition through Adjusting Substrate Preferences to Temperature

• Main Authors: Sylwia Klińska, Kamil Demski, Katarzyna Jasieniecka-Gazarkiewicz, Antoni Banaś
• Format: Article
• Language: English
• Published: MDPI AG 2021-07-01
• Series: International Journal of Molecular Sciences
• Subjects: LPEAT; LPLAT; phospholipid; abiotic stress; heat stress; cold stress
• Online Access: https://www.mdpi.com/1422-0067/22/15/8137

Acyl-CoA:lysophosphatidylethanolamine acyltransferases (LPEATs) are known as enzymes utilizing acyl-CoAs and lysophospholipids to produce phosphatidylethanolamine. Recently, it has been discovered that they are also involved in the growth regulation of <i>Arabidopsis thaliana</i>. In our study we investigated expression of each <i>Camelina sativa</i> LPEAT isoform and their behavior in response to temperature changes. In order to conduct a more extensive biochemical evaluation we focused both on LPEAT enzymes present in microsomal fractions from <i>C. sativa</i> plant tissues, and on cloned <i>Cs</i>LPEAT isoforms expressed in yeast system. Phylogenetic analyses revealed that <i>Cs</i>LPEAT1c and <i>Cs</i>LPEAT2c originated from <i>Camelina hispida</i>, whereas other isoforms originated from <i>Camelina neglecta</i>. The expression ratio of all CsLPEAT1 isoforms to all CsLPEAT2 isoforms was higher in seeds than in other tissues. The isoforms also displayed divergent substrate specificities in utilization of LPE; CsLPEAT1 preferred 18:1-LPE, whereas <i>Cs</i>LPEAT2 preferred 18:2-LPE. Unlike <i>Cs</i>LPEAT1, <i>Cs</i>LPEAT2 isoforms were specific towards very-long-chain fatty acids. Above all, we discovered that temperature strongly regulates LPEATs activity and substrate specificity towards different acyl donors, making LPEATs sort of a sensor of external thermal changes. We observed the presented findings not only for LPEAT activity in plant-derived microsomal fractions, but also for yeast-expressed individual <i>Cs</i>LPEAT isoforms.