Carnivorous plants, such as the Venus flytrap (Dionaea muscipula), depend on an animal diet when grown in nutrient-poor soils. When an insect visits the trap and tilts the mechanosensors on the inner surface, action potentials (APs) are fired. After a moving object elicits two APs, the trap snaps shut, encaging the victim. Panicking preys repeatedly touch the trigger hairs over the subsequent hours, leading to a hermetically closed trap, which via the gland-based endocrine system is flooded by a prey-decomposing acidic enzyme cocktail. Here, we asked the question as to how many times trigger hairs have to be stimulated (e.g., now many APs are required) for the flytrap to recognize an encaged object as potential food, thus making it worthwhile activating the glands. By applying a series of trigger-hair stimulations, we found that the touch hormone jasmonic acid (JA) signaling pathway is activated after the second stimulus, while more than three APs are required to trigger an expression of genes encoding prey-degrading hydrolases, and that this expression is proportional to the number of mechanical stimulations. A decomposing animal contains a sodium load, and we have found that these sodium ions enter the capture organ via glands. We identified a flytrap sodium channel DmHKT1 as responsible for this sodium acquisition, with the number of transcripts expressed being dependent on the number of mechano-electric stimulations. Hence, the number of APs a victim triggers while trying to break out of the trap identifies the moving prey as a struggling Na(+)-rich animal and nutrition for the plant.
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http://dx.doi.org/10.1016/j.cub.2015.11.057 | DOI Listing |
Planta
January 2025
Institute of Plant Genetics and Biotechnology, Plant Science and Biodiversity Center, Slovak Academy of Sciences, Akademicka 2, P. O. Box 39A, 950 07, Nitra, Slovak Republic.
DbChitI-3, Drosera binata's acidic chitinase, peaks at pH 2.5 from 15 °C to 30 °C. Gene expression is stimulated by polysaccharides and suppressed by monosaccharide digestion, implying a feedback loop in its transcriptional regulation.
View Article and Find Full Text PDFJ Chem Inf Model
December 2024
Department of Chemistry & Chemical Biology, Indian Institute of Technology (ISM) Dhanbad, Dhanbad 826004, India.
Since their inception in antibacterial therapy, macrolide-based antibiotics have significantly shaped the evolutionary pathways of pathogenic bacteria, driving them to develop diverse antimicrobial resistance (AMR) mechanisms. Among these, macrolide esterase, commonly referred to as erythromycin esterase, emerged as a critical defense mechanism, enabling bacteria to detoxify macrolides by hydrolyzing the macrolactone ring within the bacterial cell. In this study, we delve into the intricate interactions and conformational dynamics of erythromycin esterase C (EreC), a key member of the Ere enzyme family.
View Article and Find Full Text PDFProc Natl Acad Sci U S A
November 2024
Department of Molecular and Cellular Physiology, Stanford University School of Medicine, Stanford, CA 94305.
Advances in singe-particle cryo-electron microscopy (cryo-EM) have made it possible to solve the structures of numerous Family A and Family B G protein-coupled receptors (GPCRs) in complex with G proteins and arrestins, as well as several Family C GPCRs. Determination of these structures has been facilitated by the presence of large extramembrane components (such as G protein, arrestin, or Venus flytrap domains) in these complexes that aid in particle alignment during the processing of the cryo-EM data. In contrast, determination of the inactive state structure of Family A GPCRs is more challenging due to the relatively small size of the seven transmembrane domain (7TM) and to the surrounding detergent micelle that, in the absence of other features, make particle alignment impossible.
View Article and Find Full Text PDFMol Biochem Parasitol
December 2024
Institute of Medical Biochemistry Leopoldo de Meis, Federal University of Rio de Janeiro, Av. Brigadeiro Trompowsky, Rio de Janeiro 21941-590, Brazil. Electronic address:
The protozoan parasite Trypanosoma brucei possesses a large family of transmembrane receptor-like adenylate cyclases (RACs), primarily located to the flagellar surface and involved in sensing of the extracellular environment. RACs exhibit a conserved topology characterized by a large N-terminal extracellular moiety harbouring two Venus Flytrap (VFT) bilobate structures separated from an intracellular catalytic domain by a single transmembrane helix. RAC activation, which typically occurs under mild acid stress, requires the dimerization of the intracellular catalytic domain.
View Article and Find Full Text PDFCurr Biol
October 2024
Department of Biological Sciences, The National University of Singapore, Singapore 117543, Singapore; Mechanobiology Institute, The National University of Singapore, Singapore 117543, Singapore. Electronic address:
If you ever forget to water your houseplant, you may find its leaves getting soft and droopy - if you water it again in time, the leaves may stiffen, spring back up, and resist gravity. During this recovery, plant cells absorb water and build up an intracellular pressure, called turgor pressure, similar to inflating a balloon. Turgor pressure is an intrinsic component of plant physiology, and its biomechanical role as the 'hydroskeleton' is generally appreciated either statically in structural stability, like leaves resisting gravity, or dynamically in rapid motions, like Venus flytrap snapping, Mimosa closing, or stomatal opening.
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