LPEATs Tailor Plant Phospholipid Composition through Adjusting Substrate Preferences to Temperature

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 Arabidopsis thaliana. In our study we investiga...

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Bibliographic Details
Published in:International journal of molecular sciences 2021-08, Vol.22 (15), p.8137
Main Authors: Klińska, Sylwia, Demski, Kamil, Jasieniecka-Gazarkiewicz, Katarzyna, Banaś, Antoni
Format: Article
Language:English
Subjects:
abiotic stress
Apoptosis
Biosynthesis
Camelina
cold stress
Editing
Enzymes
Fatty acids
heat stress
Isoforms
LPEAT
LPLAT
Phosphatidylethanolamine
phospholipid
Phospholipid composition
Phospholipids
Phylogeny
Physiology
Plants
Preferences
Proteins
Seeds
Substrate preferences
Substrate specificity
Temperature effects
Temperature preferences
Yeast
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Summary: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 Arabidopsis thaliana. In our study we investigated expression of each Camelina sativa 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 C. sativa plant tissues, and on cloned CsLPEAT isoforms expressed in yeast system. Phylogenetic analyses revealed that CsLPEAT1c and CsLPEAT2c originated from Camelina hispida, whereas other isoforms originated from Camelina neglecta. 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 CsLPEAT2 preferred 18:2-LPE. Unlike CsLPEAT1, CsLPEAT2 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 CsLPEAT isoforms.
ISSN:1422-0067
1661-6596
1422-0067
DOI:10.3390/ijms22158137