PECTIN METHYLESTERASE INHIBITOR18 functions in stomatal dynamics and stomatal dimension.

Pectin methylesterification in guard cell (GC) walls plays an important role in stomatal development and stomatal response to external stimuli, and pectin methylesterase inhibitors (PMEIs) modulate pectin methylesterification by inhibition of pectin methylesterase (PME). However, the function of PMEIs has not been reported in stomata. Here, we report the role of Arabidopsis (Arabidopsis thaliana) PECTIN METHYLESTERASE INHIBITOR18 in stomatal dynamic responses to environmental changes. PMEI18 mutation increased pectin demethylesterification and reduced pectin degradation, resulting in increased stomatal pore size, impaired stomatal dynamics, and hypersensitivity to drought stresses. In contrast, overexpression of PMEI18 reduced pectin demethylesterification and increased pectin degradation, causing more rapid stomatal dynamics. PMEI18 interacted with PME31 in plants, and in vitro enzymatic assays demonstrated that PMEI18 directly inhibits the PME activity of PME31 on pectins. Genetic interaction analyses suggested that PMEI18 modulates stomatal dynamics mainly through inhibition of PME31 on pectin methylesterification in cell walls. Our results provide insight into the molecular mechanism of the PMEI18-PME31 module in stomatal dynamics and highlight the role of PMEI18 and PME31 in stomatal dynamics through modulation of pectin methylesterification and distribution in GC walls.

Modulation of broiler plasma metabolic spectrum by the addition of lysine residue to the diet.

Flavour is an important factor in evaluating meat quality, and amino acids and fats are important components affecting meat flavour. In this study, we evaluated the relationship between the variation of lysine residue addition and the slaughter performance and meat quality of broilers, which decreased with the addition of lysine residues but improved the meat quality of the broilers. 10% lysine residue addition was the most beneficial for reducing feed cost and improving meat quality. Meanwhile, the plasma metabolites of broilers fed increasing concentrations of lysine residue supplemented feeds were analysed using liquid chromatography-mass spectrometry (LC-MS). Principal component analysis (PCA) and partial least square discriminant analysis (OPLS-DA) were used screen, the differential metabolites induced by lysine residue. In the broilers 29, 37, 63, 87, 80 and 111 differential metabolites were detected (p < 0.05). Amongst them, 3-iodotyrosine, N-methyl-L-glutamic acid, coumaraldehyde, 2-dimethylphenol, N-methylnicotinamide and L-erythrone were the common differential metabolites between group A and groups B, C, D, E, F and G. The addition of lysine residue was positively correlated with alanine aminotransferase (p < 0.05, r = 0.942) and high-density lipoprotein cholesterol (p < 0.05, r = 0.798) and negatively correlated with aspartate aminotransferase (p < 0.05, r = 0.822). According to the classification of differential metabolites and their enriched pathway analysis, differential metabolites mainly caused changes in amino acid and lipid metabolism. Our study shows that a certain proportion of lysine residue in diet affects the specific metabolic pathway of broilers, which may affect amino acid and fat metabolism by regulating alanine aminotransferase, aspartate aminotransferase and high-density lipoprotein cholesterol, ultimately affecting the flavour.

Two types of soybean diacylglycerol acyltransferases are differentially involved in triacylglycerol biosynthesis and response to environmental stresses and hormones.

Diacylglycerol acyltransferases (DGATs) play a key role in plant triacylglycerol (TAG) biosynthesis. Two type 1 and 2 DGATs from soybean were characterized for their functions in TAG biosynthesis and physiological roles. GmDGAT1A is highly expressed in seeds while GmDGAT2D is mainly expressed in flower tissues. They showed different expression patterns in response to biotic and abiotic stresses. GmDGAT2D was up-regulated by cold and heat stress and ABA signaling, and repressed by insect biting and jasmonate, whereas GmDGAT1A show fewer responses. Both GmDGAT1A and GmDGAT2D were localized to the endoplasmic reticulum and complemented the TAG deficiency of a yeast mutant H1246. GmDGAT2D-transgenic hairy roots synthesized more 18:2- or 18:1-TAG, whereas GmDGAT1A prefers to use 18:3-acyl CoA for TAG synthesis. Overexpression of both GmDGATs in Arabidopsis seeds enhanced the TAG production; GmDGAT2D promoted 18:2-TAG in wild-type but enhanced 18:1-TAG production in rod1 mutant seeds, with a decreased 18:3-TAG. However, GmDGAT1A enhanced 18:3-TAG and reduced 20:1-TAG contents. The different substrate preferences of two DGATs may confer diverse fatty acid profiles in soybean oils. While GmDGAT1A may play a role in usual seed TAG production and GmDGAT2D is also involved in usual TAG biosynthesis in other tissues in responses to environmental and hormonal cues.