Acyl Moiety Research Articles

A Set of Highly Sensitive Sirtuin Fluorescence Probes for Screening Small-Molecular Sirtuin Defatty-Acylase Inhibitors.

Human sirtuins (SIRT1-7) regulate not only deacetylation but also deacylation of fatty acid-derived acyl moieties (defatty-acylation) at the ε-amino group of lysine residues. SIRT-subtype-specific defatty-acylase activity modulators are needed for detailed investigation of the biological roles of these enzymes, and to find suitable small molecules, we require appropriate screening systems. Here, we designed and synthesized a set of SIRT defatty-acylase activity probes with various quencher moieties and peptide sequences based on our previously developed one-step FRET-based SIRT probe SFP3, using improved methodology. Scanning of this set of probes with SIRT isozymes revealed that certain probe/isozyme combinations showed especially high responses. To illustrate the utility of the combinations thus identified, we applied compound 18/SIRT2 for inhibitor screening of a large chemical library. This enabled us to discover a new small molecule SIRT2-specific defatty-acylase inhibitor.

Asymmetric glycerophospholipids impart distinctive biophysical properties to lipid bilayers

Phospholipids are a diverse group of biomolecules consisting of a hydrophilic headgroup and two hydrophobic acyl tails. The nature of the head and length and saturation of the acyl tails are important for defining the biophysical properties of lipid bilayers. It has recently been shown that the membranes of certain yeast species contain high levels of unusual asymmetric phospholipids consisting of one long and one medium-chain acyl moiety, a configuration not common in mammalian cells or other well-studied model yeast species. This raises the possibility that structurally asymmetric glycerophospholipids impart distinctive biophysical properties to the yeast membranes. Previously, it has been shown that lipids with asymmetric length tails form a mixed interdigitated gel phase and exhibit unusual endotherm behavior upon heating and cooling. Here, however, we address physiologically relevant temperature conditions and, using atomistic molecular dynamics simulations and environmentally sensitive fluorescent membrane probes, characterize key biophysical parameters (such as lipid packing, diffusion coefficient, membrane thickness, and area per lipid) in membranes composed of both length-asymmetric glycerophospholipids and ergosterol. Interestingly, we show that saturated but asymmetric glycerophospholipids maintain membrane lipid order across a wide range of temperatures. We also show that these asymmetric lipids can substiture of unsaturated symmetric lipids in the phase behaviour of ternary lipid bilayers. This may allow cells to maintain membrane fluidity, even in environments that lack oxygen, which is required for the synthesis of unsaturated lipids and sterols.

Structure—Activity Relationship of Local Anesthetics Based on Alkynylpiperidine Derivatives

The influence of the nature of the acyl (propionyl and benzoyl) moiety and the piperidine ring C4 substituent on the activity of several alkynylpiperidine derivatives was studied. The presence of an alkyl (hexyl) radical on the triple bond of the piperidine ring C4 substituent in the infiltration anesthesia model had a positive effect on the anesthesia index and the duration of both total and general anesthesia as compared to lidocaine, novocaine, and trimecaine taken as reference drugs. The ester of 4-(octyn-1-yl)piperidol-1-propionic acid was the most active anesthetic among the studied compounds. Modification of the triple bond (exhaustive hydrogenation and hydration) led to a decrease in the duration of anesthesia. The activity of the benzoate was greater than that of the propionate in the propionate-benzoate pair.

Receptor-binding affinity and larvicidal activity of tetrahydroquinoline-type ecdysone agonists against Aedes albopictus.

Tetrahydroquinolines (THQs), a class of nonsteroidal ecdysone agonists, are good candidates for novel mosquito control agents because they specifically bind to mosquito ecdysone receptors (EcRs). We have recently performed quantitative structure–activity relationship (QSAR) analyses of THQs to elucidate the physicochemical properties important for the ligand–receptor interaction. Based on previous QSAR results, here, we newly synthesized 15 THQ analogs with a heteroaryl group at the acyl moiety and evaluated their binding affinity against Aedes albopictus EcRs. We also measured the larvicidal activity of the combined set of previously and newly synthesized compounds against A. albopictus to examine the contribution of receptor-binding to larvicidal activity. Multiple regression analyses showed that the binding affinity and the molecular hydrophobicity of THQs are the key determinants of their larvicidal activity.

Lipases of germinating jojoba seeds efficiently hydrolyze triacylglycerols and wax esters and display wax ester-synthesizing activity

BackgroundSimmondsia chinensis (jojoba) is the only plant known to store wax esters instead of triacylglycerols in its seeds. Wax esters are composed of very-long-chain monounsaturated fatty acids and fatty alcohols and constitute up to 60% of the jojoba seed weight. During jojoba germination, the first step of wax ester mobilization is catalyzed by lipases. To date, none of the jojoba lipase-encoding genes have been cloned and characterized. In this study, we monitored mobilization of storage reserves during germination of jojoba seeds and performed detailed characterization of the jojoba lipases using microsomal fractions isolated from germinating seeds.ResultsDuring 26 days of germination, we observed a 60–70% decrease in wax ester content in the seeds, which was accompanied by the reduction of oleosin amounts and increase in glucose content. The activity of jojoba lipases in the seed microsomal fractions increased in the first 50 days of germination. The enzymes showed higher activity towards triacylglycerols than towards wax esters. The maximum lipase activity was observed at 60 °C and pH around 7 for triacylglycerols and 6.5–8 for wax esters. The enzyme efficiently hydrolyzed various wax esters containing saturated and unsaturated acyl and alcohol moieties. We also demonstrated that jojoba lipases possess wax ester-synthesizing activity when free fatty alcohols and different acyl donors, including triacylglycerols and free fatty acids, are used as substrates. For esterification reactions, the enzyme utilized both saturated and unsaturated fatty alcohols, with the preference towards long chain and very long chain compounds.ConclusionsIn in vitro assays, jojoba lipases catalyzed hydrolysis of triacylglycerols and different wax esters in a broad range of temperatures. In addition, the enzymes had the ability to synthesize wax esters in the backward reaction. Our data suggest that jojoba lipases may be more similar to other plant lipases than previously assumed.

Synthesis of new series of pyrimidine nucleoside derivatives bearing the acyl moieties as potential antimicrobial agents

Nucleoside derivatives are important therapeutic drugs and are the focal point in the ongoing search for novel, more potent drug targets. In this study, a new series of pyrimidine nucleoside i.e., uridine (1) derivatives were synthesized via direct method and evaluated for their antimicrobial potential activity. The title compound uridine (1) was treated with triphenylmethyl chloride in pyridine to give the 5´-O-(triphenylmethyl)uridine derivative (2), which was subsequently derivatized to create a series of 2´,3´-di-O-acyl analogs containing a wide variety of functionalities in a single molecular framework. In vitro antimicrobial functionality tests were determined against both human and plant pathogens by disc diffusion and food poisoned techniques. The chemical structures of the synthesized compounds were confirmed on the basis of their spectral, analytical, physicochemical data. The antimicrobial results indicated that the synthesized derivatives exhibited moderate to good antibacterial and antifungal activity; in particular, they were found to be more effective against fungal phytopathogens than against human bacterial strains. Compounds 7, 9, and 14 were of particular interest as they exhibited noteworthy antifungal and antibacterial properties. In vitro MTT assays revealed that compound 9 was effective against Ehrlich’s ascites carcinoma (EAC) cells, resulting in 7.12% and 1.34% cell growth inhibition at concentrations of 200 and 6.25 µg/ml, respectively. The IC50 value for compound 9 was rather high and found to be 1956.25 µg/ml. Structure-activity relationship (SAR) studies were also conducted to predict structural and pharmacokinetic properties. The findings of this study indicate that the different uridine derivatives are potentially useful antimicrobial agents for the advancement of future pharmaceutical research.

Approaches for the synthesis, chemical modification and biological properties of N-acylphenothiazines

In this review we systematized the theoretical and experimental data concerning the versatile approaches for the synthesis of N-acylphenothiazines. The aim of the study was to compile the literature reported worldwide in the past 20 years. This article also reviewed the analysis of pharmacological activities of these heterocycles as one of the promising chemotherapeutic objects for the modern bioorganic and medicinal chemistry. It has been hypothesized that the enormous biological potential of these moieties is due to the radical nature in the acyl moiety. Therefore, the present review will be a good contribution to the literature and will provide the platform for the medicinal chemistry researchers to carry out more studies aiming the N-acylphenothiazine moieties as the novel chemotherapeutic agents.

Classification and phylogeny for the annotation of novel eukaryotic GNAT acetyltransferases.

The enzymes of the GCN5-related N-acetyltransferase (GNAT) superfamily count more than 870 000 members through all kingdoms of life and share the same structural fold. GNAT enzymes transfer an acyl moiety from acyl coenzyme A to a wide range of substrates including aminoglycosides, serotonin, glucosamine-6-phosphate, protein N-termini and lysine residues of histones and other proteins. The GNAT subtype of protein N-terminal acetyltransferases (NATs) alone targets a majority of all eukaryotic proteins stressing the omnipresence of the GNAT enzymes. Despite the highly conserved GNAT fold, sequence similarity is quite low between members of this superfamily even when substrates are similar. Furthermore, this superfamily is phylogenetically not well characterized. Thus functional annotation based on sequence similarity is unreliable and strongly hampered for thousands of GNAT members that remain biochemically uncharacterized. Here we used sequence similarity networks to map the sequence space and propose a new classification for eukaryotic GNAT acetyltransferases. Using the new classification, we built a phylogenetic tree, representing the entire GNAT acetyltransferase superfamily. Our results show that protein NATs have evolved more than once on the GNAT acetylation scaffold. We use our classification to predict the function of uncharacterized sequences and verify by in vitro protein assays that two fungal genes encode NAT enzymes targeting specific protein N-terminal sequences, showing that even slight changes on the GNAT fold can lead to change in substrate specificity. In addition to providing a new map of the relationship between eukaryotic acetyltransferases the classification proposed constitutes a tool to improve functional annotation of GNAT acetyltransferases.

Deoxyfluorination of acyl fluorides to trifluoromethyl compounds by FLUOLEAD®/Olah's reagent under solvent-free conditions.

A new protocol enabling the formation of trifluoromethyl compounds from acyl fluorides has been developed. The combination of FLUOLEAD® and Olah’s reagent in solvent-free conditions at 70 °C initiated the significant deoxyfluorination of the acyl fluorides and resulted in the corresponding trifluoromethyl products with high yields (up to 99%). This strategy showed a great tolerance for various acyl fluorides containing aryloyl, (heteroaryl)oyl, or aliphatic acyl moieties, providing good to excellent yields of the trifluoromethyl products. Synthetic drug-like molecules were also transformed into the corresponding trifluoromethyl compounds under the same reaction conditions. A reaction mechanism is proposed.

Nucleotide-binding sites can enhance N-acylation of nearby protein lysine residues

Acyl-CoAs are reactive metabolites that can non-enzymatically S-acylate and N-acylate protein cysteine and lysine residues, respectively. N-acylation is irreversible and enhanced if a nearby cysteine residue undergoes an initial reversible S-acylation, as proximity leads to rapid S → N-transfer of the acyl moiety. We reasoned that protein-bound acyl-CoA could also facilitate S → N-transfer of acyl groups to proximal lysine residues. Furthermore, as CoA contains an ADP backbone this may extend beyond CoA-binding sites and include abundant Rossmann-fold motifs that bind the ADP moiety of NADH, NADPH, FADH and ATP. Here, we show that excess nucleotides decrease protein lysine N-acetylation in vitro. Furthermore, by generating modelled structures of proteins N-acetylated in mouse liver, we show that proximity to a nucleotide-binding site increases the risk of N-acetylation and identify where nucleotide binding could enhance N-acylation in vivo. Finally, using glutamate dehydrogenase as a case study, we observe increased in vitro lysine N-malonylation by malonyl-CoA near nucleotide-binding sites which overlaps with in vivo N-acetylation and N-succinylation. Furthermore, excess NADPH, GTP and ADP greatly diminish N-malonylation near their nucleotide-binding sites, but not at distant lysine residues. Thus, lysine N-acylation by acyl-CoAs is enhanced by nucleotide-binding sites and may contribute to higher stoichiometry protein N-acylation in vivo.

Biosynthesis of depsipeptides, or Depsi: The peptides with varied generations.

Depsipeptides are compounds that contain both ester bonds and amide bonds. Important natural product depsipeptides include the piscicide antimycin, the K+ ionophores cereulide and valinomycin, the anticancer agent cryptophycin, and the antimicrobial kutzneride. Furthermore, database searches return hundreds of uncharacterized systems likely to produce novel depsipeptides. These compounds are made by specialized nonribosomal peptide synthetases (NRPSs). NRPSs are biosynthetic megaenzymes that use a module architecture and multi-step catalytic cycle to assemble monomer substrates into peptides, or in the case of specialized depsipeptide synthetases, depsipeptides. Two NRPS domains, the condensation domain and the thioesterase domain, catalyze ester bond formation, and ester bonds are introduced into depsipeptides in several different ways. The two most common occur during cyclization, in a reaction between a hydroxy-containing side chain and the C-terminal amino acid residue in a peptide intermediate, and during incorporation into the growing peptide chain of an α-hydroxy acyl moiety, recruited either by direct selection of an α-hydroxy acid substrate or by selection of an α-keto acid substrate that is reduced in situ. In this article, we discuss how and when these esters are introduced during depsipeptide synthesis, survey notable depsipeptide synthetases, and review insight into bacterial depsipeptide synthetases recently gained from structural studies.

The specific features of the liquid-phase oxidation of saturated esters. Kinetics, reactivity and mechanisms of formation of destruction products

Data on kinetics, reactivity, and mechanisms of formation of destruction products of the liquid-phase oxidation of saturated esters by molecular oxygen have been systematized and discussed. The ester group has both an activating and deactivating effects on the reactivity of the CH bonds of the alkoxyl (α′-, β′-, γ′-, and δ′-) and acyl (α-, β-, and γ-) groups. The activating effect in esters is weaker than in alcohols, ketones, and ethers and extends to the α- and α′-CH bonds. The reactivity of the β-, β′-, and γ′-CH bonds is significantly lower than that of the secondary CH bonds of hydrocarbons. Oxidation of the β-CH bonds of the acyl moieties of esters leads to HOO· radical, α,β-epoxy-, α,β-dihydroxy-, and α,β-unsaturated esters, but not to hydroperoxides. Upon the oxidation of esters, the highly active α-carboxy-alkylperoxy-, α-acyloxyperoxy-, and HOO· -radicals are formed. The recombination reactions involving these radicals occur both with and without chain termination. The specificity of the decomposition of ester hydroperoxides are due to intra- and intermolecular interactions of the hydroperoxide groups with the ester groups. Labile peroxide intermediates (α-hydroxyperoxy-esters, peroxyesters, and peroxylactones) are formed through the corresponding tetrahedral intermediates and decay predominantly by the non-radical pathway. The recombination of the peroxyl radicals and the decay of labile peroxides result in the parallel accumulation of peroxide and non-peroxide products during the oxidation of esters.

Characteristics and origin of intact polar lipids in soil organic matter

Membrane lipids and their related acyl and/or alkyl moieties are important biomarkers of the microbial community in environmental samples. Intact polar lipids, which are described by their lipid head groups and fatty acid tails, are major membrane components of living cells only and may therefore provide information about the living soil microbial community. However, the intact polar lipids in soil organic matter may originate from non-microbial organisms (e.g., roots, soil animals) as well as microorganisms. We report on the profiles of more than 300 membrane-derived intact polar lipids in grassland soil organic matter from sites with diverse plant communities and soil properties. The origin of the soil lipid profiles was deduced by comparisons with the intact polar lipids of plant roots, amoebae, collembolans, fungi and bacteria. In addition, we investigated the impact of plant and soil-related drivers on the composition of the intact polar lipids in soil organic matter. Soil organic matter lipid profiles were considerably more diverse and evenly distributed than the profiles of roots and soil organisms (amoebae, bacteria, collembolans and fungi). Moreover, the lipid profiles in soil organic matter had more odd-carbon numbered acyl and alkyl chains, ornithine lipids, and phospholipids with low levels of unsaturation, possibly because they are of bacterial origin. We suggest that most of the intact polar lipids in soil organic matter (45–80%) were derived from bacteria, rather than plants, fungi, or soil animals. The PE (31:0) and PE (32:1) lipids were considered as biomarkers for all bacteria, whereas PE (29:0, 29:2 and 30:0) are specific to Gram (+) bacteria and PG (33; 0, 34:1 and 36:2) and OL (36:0, 37:0, 37:1, 39:1 and 39:2) were used to identify Gram (−) bacteria. Bacterial lipids were differentiated from intact lipids of plant roots that typically contain MGDG (36:4) and MGDG (36:6), while fungi have indicative markers of PC (36:4) and PE (36:4). Thus, intact polar lipid profiles complement and advance other approaches, such as fatty acid-based analysis of soil microbial community composition, and may allow for analysis of soil food web structure.

Uncovering the complexity of the yeast lipidome by means of nLC/NSI-MS/MS

Saccharomyces cerevisiae is a eukaryotic model organism widely used for the investigation of fundamental cellular processes and disease mechanisms. Consequently, the lipid landscape of yeast has been extensively investigated and up to this day the lipidome is considered as rather basic. Here, we used a nLC/NSI-MS/MS method combined with a semi-autonomous data analysis workflow for an in-depth evaluation of the steady state yeast lipidome. We identified close to 900 lipid species across 26 lipid classes, including glycerophospholipids, sphingolipids, glycerolipids and sterol lipids. Most lipid classes are dominated by few high abundant species, with a multitude of lower abundant lipids contributing to the overall complexity of the yeast lipidome. Contrary to previously published datasets, odd-chain and diunsaturated fatty acyl moieties were found to be commonly incorporated in multiple lipid classes. Careful data evaluation furthermore revealed the presence of putative new lipid species such as MMPSs (mono-methylated phosphatidylserine), not yet described in yeast. Overall, our analysis achieved a more than 4-fold increase in lipid identifications compared to previous approaches, underscoring the use of nLC/NSI-MS/MS methods for the in-depth investigation of lipidomes.

Electrospray ionization with higher-energy collision dissociation tandem mass spectrometry toward characterization of ceramides as [M + Li]+ ions: Mechanisms of fragmentation and structural identification

Ceramide is a huge lipid family consisting of diversified structures in which various modifications are seen in the fatty acyl chain and the long chain base (LCB). In this contribution, a higher collision energy (HCD) linear ion-trap mass spectrometric method (LIT MSn) was applied to study the mechanisms underlying the fragmentation processes of ceramide molecules in 12 subclasses, which were desorbed by ESI as the [M + Li]+ ions. Multiple sets of fragment ions reflecting the fatty acyl chain and LCB were observed in the HCD MS2 spectra for all the ceramide classes, resulting in unambiguous definition of the ceramide structures, including the chain length and the modification (α-hydroxy-, β-hydroxy-, ω-hydroxy-FA) of the fatty acyl moiety, and the types of LCB (sphingosine, phytosphigosine, 6-hydroxy-sphingosine). Thereby, this approach permits differentiation of isomeric structures and ceramide species in the biological specimen can be unveiled in detail. By application of sequential MS3, the double bond position along the fatty acyl chain of the molecule can be located, and a complete structural characterization of ceramides can be achieved.

Characterization of the acyl-ACP thioesterases from Koelreuteria paniculata reveals a new type of FatB thioesterase

Koelreuteria paniculata is a deciduous tree, popular in temperate regions for its ornamental value, which accumulates unusual cyanolipids in its seeds. The seed oil of this plant is rich in the unusual cis-11-eicosenoic fatty acid (20:1, or gondoic acid), a monounsaturated oil of interest to the oleochemical industry. In higher plants, de novo fatty acid biosynthesis takes place in the plastids, a process that is terminated by hydrolysis of the thioester bond between the acyl moiety and the ACP by acyl-ACP thioesterases. The specificity of acyl-ACP thioesterases is fundamental in controlling the fatty acid composition of seed oil. To determine the mechanisms involved in fatty acid biosynthesis in K. paniculata seeds, we isolated, cloned and sequenced two cDNAs encoding acyl-ACP thioesterases in this plant, KpFatA and KpFatB. Both of them were expressed heterologously in Escherichia coli and characterized with different acyl-ACP substrates. The K. paniculata FatB2 displayed unusual substrate specificity, so that unlike most FatB2 type enzymes, it displayed preference for oleoyl-ACP instead of palmitoyl-ACP. This specificity was consistent with the changes in E. coli and N. benthamiana fatty acid composition following heterologous expression of this enzyme. KpFatB also showed certain genetic divergence relative to other FatB-type thioesterases and when modelled, its structure revealed differences at the active site. Together, these results suggest that this thioesterase could be a new class of FatB not described previously.

Automated Annotation of Sphingolipids Including Accurate Identification of Hydroxylation Sites Using MSn Data.

Sphingolipids constitute a heterogeneous lipid category that is involved in many key cellular functions. For high-throughput analyses of sphingolipids, tandem mass spectrometry (MS/MS) is the method of choice, offering sufficient sensitivity, structural information, and quantitative precision for detecting hundreds to thousands of species simultaneously. While glycerolipids and phospholipids are predominantly non-hydroxylated, sphingolipids are typically dihydroxylated. However, species containing one or three hydroxylation sites can be detected frequently. This variability in the number of hydroxylation sites on the sphingolipid long-chain base and the fatty acyl moiety produces many more isobaric species and fragments than for other lipid categories. Due to this complexity, the automated annotation of sphingolipid species is challenging, and incorrect annotations are common. In this study, we present an extension of the Lipid Data Analyzer (LDA) “decision rule set” concept that considers the structural characteristics that are specific for this lipid category. To address the challenges inherent to automated annotation of sphingolipid structures from MS/MS data, we first developed decision rule sets using spectra from authentic standards and then tested the applicability on biological samples including murine brain and human plasma. A benchmark test based on the murine brain samples revealed a highly improved annotation quality as measured by sensitivity and reliability. The results of this benchmark test combined with the easy extensibility of the software to other (sphingo)lipid classes and the capability to detect and correctly annotate novel sphingolipid species make LDA broadly applicable to automated sphingolipid analysis, especially in high-throughput settings.

Carnitine Traffic in Cells. Link With Cancer.

Metabolic flexibility is a peculiar hallmark of cancer cells. A growing number of observations reveal that tumors can utilize a wide range of substrates to sustain cell survival and proliferation. The diversity of carbon sources is indicative of metabolic heterogeneity not only across different types of cancer but also within those sharing a common origin. Apart from the well-assessed alteration in glucose and amino acid metabolisms, there are pieces of evidence that cancer cells display alterations of lipid metabolism as well; indeed, some tumors use fatty acid oxidation (FAO) as the main source of energy and express high levels of FAO enzymes. In this metabolic pathway, the cofactor carnitine is crucial since it serves as a “shuttle-molecule” to allow fatty acid acyl moieties entering the mitochondrial matrix where these molecules are oxidized via the β-oxidation pathway. This role, together with others played by carnitine in cell metabolism, underlies the fine regulation of carnitine traffic among different tissues and, within a cell, among different subcellular compartments. Specific membrane transporters mediate carnitine and carnitine derivatives flux across the cell membranes. Among the SLCs, the plasma membrane transporters OCTN2 (Organic cation transport novel 2 or SLC22A5), CT2 (Carnitine transporter 2 or SLC22A16), MCT9 (Monocarboxylate transporter 9 or SLC16A9) and ATB0, + [Sodium- and chloride-dependent neutral and basic amino acid transporter B(0+) or SLC6A14] together with the mitochondrial membrane transporter CAC (Mitochondrial carnitine/acylcarnitine carrier or SLC25A20) are the most acknowledged to mediate the flux of carnitine. The concerted action of these proteins creates a carnitine network that becomes relevant in the context of cancer metabolic rewiring. Therefore, molecular mechanisms underlying modulation of function and expression of carnitine transporters are dealt with furnishing some perspective for cancer treatment.

Ruthenium‐Based Structural Mimics of the Cofactor of [Fe]‐Hydrogenase: Replacement of the Acyl Moiety with an N‐Heterocyclic Carbene

AbstractA synthetic route is reported towards ruthenium‐based structural mimics of the [Fe]‐hydrogenase metal cofactor in which the acyl moiety is replaced by an N‐heterocyclic carbene. It is observed that the pyridyl‐NHC ligand has a rather different trans influence from that of a simple NHC in their ruthenium derivatives. The basis for this difference is explored crystallographically and computationally, and it accounts for their different behaviour towards thiolation.

Plastid Glycerol-3-phosphate Acyltransferase Enhanced Plant Growth and Prokaryotic Glycerolipid Synthesis in Brassica napus.

Plastid-localized glycerol-3-phosphate acyltransferase (ATS1) catalyzes the first-step reaction in glycerolipid assembly through transferring an acyl moiety to glycerol-3-phosphate (G3P) to generate lysophosphatidic acid (LPA), an intermediate in lipid metabolism. The effect of ATS1 overexpression on glycerolipid metabolism and growth remained to be elucidated in plants, particularly oil crop plants. Here, we found that overexpression of BnATS1 from Brassica napus enhanced plant growth and prokaryotic glycerolipid biosynthesis. BnATS1 is localized in chloroplasts and an in vitro assay showed that BnATS1 had acylation activity toward glycerol 3-phosphate to produce LPA. Lipid profiling showed that overexpression of BnATS1 led to increases in multiple glycerolipids including phosphatidylglycerol (PG), monogalactosyldiacylglycerol (MGDG), phosphatidylcholine (PC), and phosphatidylinositol (PI), with increased polyunsaturated fatty acids. Moreover, increased MGDG was attributed to the elevation of 34:6- and 34:5-MGDG, which were derived from the prokaryotic pathway. These results suggest that BnATS1 promotes accumulation of polyunsaturated fatty acids in cellular membranes, thus enhances plant growth under low-temperature conditions in Brassica napus.