Plant stomata function in innate immunity against bacterial invasion and abscisic acid (ABA) has been suggested to regulate this process. Using genetic, biochemical, and pharmacological approaches, we demonstrate that (i) the Arabidopsis thaliana nine-specific-lipoxygenase encoding gene, LOX1, which is expressed in guard cells, is required to trigger stomatal closure in response to both bacteria and the pathogen-associated molecular pattern flagellin peptide flg22; (ii) LOX1 participates in stomatal defense; (iii) polyunsaturated fatty acids, the LOX substrates, trigger stomatal closure; (iv) the LOX products, fatty acid hydroperoxides, or reactive electrophile oxylipins induce stomatal closure; and (v) the flg22-mediated stomatal closure is conveyed by both LOX1 and the mitogen-activated protein kinases MPK3 and MPK6 and involves salicylic acid whereas the ABA-induced process depends on the protein kinases OST1, MPK9, or MPK12. Finally, we show that the oxylipin and the ABA pathways converge at the level of the anion channel SLAC1 to regulate stomatal closure. Collectively, our results demonstrate that early biotic signaling in guard cells is an ABA-independent process revealing a novel function of LOX1-dependent stomatal pathway in plant immunity. Stomata are microscopic pores that are present in the epidermis of the aerial parts of higher plants, such as the leaves. These pores, which are flanked by a pair of cells called guard cells, regulate transpiration and the exchange of gas between leaves and the atmosphere. It is well documented that the phytohormone abscisic acid (ABA) is a key regulator that controls the osmotic pressure in guard cells, allowing pore size to be adjusted in response to environmental conditions. Recently, stomata have also been shown to play an important role in the innate immune response. Indeed, upon contact with microbes, plants actively close stomata to prevent the entry of microbes and the consequent colonization of host tissue. This response is known as the stomatal defense response. However, the molecular mechanisms that regulate this defense response are not well understood. Using a variety of approaches, we show in this study that LOX1, a gene that encodes lipoxygenase (LOX) in guard cells, plays a major role in stomatal defense in the model plant Arabidopsis thaliana. Mutations in LOX1 impair stomatal closure and make plants more susceptible to the bacterium Pseudomonas syringae pv. tomato. We also show that several LOX-derived metabolites, the oxylipins, are potent inducers of stomatal closure. Finally, we provide evidence to show that ABA plays only a minor role in stomatal defense response, specifically by modulating this response.

The basic structure of membrane glycoconjugates in Leishmania still inspires therapeutic drugs fighting against this parasite.

Hyperthermophilic Archaea colonizing unnatural habitats of extremes conditions such as volcanoes and deep-sea hydrothermal vents represent an unmeasurable bioresource for enzymes used in various industrial applications. Their enzymes show distinct structural and functional properties and are resistant to extreme conditions of temperature and pressure where their mesophilic homologs fail. In this review, we will outline carbohydrate-active enzymes (CAZymes) from hyperthermophilic Archaea with specific focus on the two largest families, glycoside hydrolases (GHs) and glycosyltransferases (GTs). We will present the latest advances on these enzymes particularly in the light of novel accumulating data from genomics and metagenomics sequencing technologies. We will discuss the contribution of these enzymes from hyperthermophilic Archaea to industrial applications and put the emphasis on newly identifed enzymes. We will highlight their common biochemical and distinct features. Finally, we will overview the areas that remain to be explored to identify novel promising hyperthermozymes.

We report here the first chemical synthesis of three depsides related to quercetinase‐catalyzed degradation of kaempferol, quercetin, and myricetin. The three depsides were constructed through the coupling of suitably protected phloroglucinol carboxylic acid and hydroxy‐perbenzylated, derivatives of gallic, protocatechuic, and 4‐hydroxy benzoic acids. The three synthesized target compounds proved to be identical to their natural counterparts, arising from quercetinase action on corresponding flavonols.