Omanische Heilpflanze im Fokus der Phytochemie IPB-Wissenschaftler und Partner aus Dhofar haben jüngst die omanische Heilpflanze Terminalia dhofarica unter die phytochemische Lupe genommen. Die Pflanze ist reich an…
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Mamadalieva, N. Z.; Hussain, H.; Xiao, J.;Recent advances in genus
Mentha
: Phytochemistry, antimicrobial effects, and food applicationsFood Frontiers1435-458(2020)DOI: 10.1002/fft2.53
The genus Mentha (mint) belongs to the Lamiaceae family, which
includes 25 to 30 species. The species of this genus have been known for their medicinal and aromatherapeutic properties since ancient times and possess a significant economical and commercial reputation. Several
species of Mentha are widely used in culinary and traditional medicines in many parts of the world. Essential oils from Mentha
species have been commonly used as flavoring substance in beverages,
providing a “fresh-like” aroma and taste. Chemical analyses of Mentha species have yielded a number of important phytocompounds belonging to different classes, such as organic acids, flavonoids, sterols, alkaloids, lignans, hydrocarbons, fatty acids, tocopherols, proteins, free sugars, etc. Moreover, the main compounds in mints are essential oils, phenolics, and flavonoids. This review reports the available information on the present status (literature up to early 2020) of the Mentha species and summarizes the chemical constituents, traditional and culinary uses, cultivation, and biological properties. In addition, comprehensive analysis of the antibacterial studies conducted on Mentha species is represented. In effect, Mentha species have been presented here as a viable alternative source of many biological and chemically active compounds which are already known to be of great economic, pharmaceutical, and nutritional importance.
Publikation
Dunker, F.; Trutzenberg, A.; Rothenpieler, J. S.; Kuhn, S.; Pröls, R.; Schreiber, T.; Tissier, A.; Kemen, A.; Kemen, E.; Hückelhoven, R.; Weiberg, A.;Oomycete small RNAs bind to the plant RNA-induced silencing complex for virulenceeLife9e56096(2020)DOI: 10.7554/eLife.56096
The exchange of small RNAs (sRNAs) between hosts and pathogens can lead to gene silencing in the recipient organism, a mechanism termed cross-kingdom RNAi (ck-RNAi). While fungal sRNAs promoting virulence are established, the significance of ck-RNAi in distinct plant pathogens is not clear. Here, we describe that sRNAs of the pathogen Hyaloperonospora arabidopsidis, which represents the kingdom of oomycetes and is phylogenetically distant from fungi, employ the host plant's Argonaute (AGO)/RNA-induced silencing complex for virulence. To demonstrate H. arabidopsidis sRNA (HpasRNA) functionality in ck-RNAi, we designed a novel CRISPR endoribonuclease Csy4/GUS reporter that enabled in situ visualization of HpasRNA-induced target suppression in Arabidopsis. The significant role of HpasRNAs together with AtAGO1 in virulence was revealed in plant atago1 mutants and by transgenic Arabidopsis expressing a short-tandem-target-mimic to block HpasRNAs, that both exhibited enhanced resistance. HpasRNA-targeted plant genes contributed to host immunity, as Arabidopsis gene knockout mutants displayed quantitative enhanced susceptibility.
Eukaryotes have evolved various quality control mechanisms to promote proteostasis in the endoplasmic reticulum (ER). Selective removal of certain ER domains via autophagy (termed as ER-phagy) has emerged as a major quality control mechanism. However, the degree to which ER-phagy is employed by other branches of ER-quality control remains largely elusive. Here, we identify a cytosolic protein, C53, that is specifically recruited to autophagosomes during ER-stress, in both plant and mammalian cells. C53 interacts with ATG8 via a distinct binding epitope, featuring a shuffled ATG8 interacting motif (sAIM). C53 senses proteotoxic stress in the ER lumen by forming a tripartite receptor complex with the ER-associated ufmylation ligase UFL1 and its membrane adaptor DDRGK1. The C53/UFL1/DDRGK1 receptor complex is activated by stalled ribosomes and induces the degradation of internal or passenger proteins in the ER. Consistently, the C53 receptor complex and ufmylation mutants are highly susceptible to ER stress. Thus, C53 forms an ancient quality control pathway that bridges selective autophagy with ribosome-associated quality control in the ER.