Natural nitrogen isotopic signature reveals deprotonation during ammonium transport across living organisms.
Diphthamide, a post-translationally modified histidine residue of eukaryotic TRANSLATION ELONGATION FACTOR2 (eEF2), is the human host cell-sensitizing target of diphtheria toxin. Diphthamide biosynthesis depends on the 4Fe-4S-cluster protein Dph1 catalyzing the first committed step, as well as Dph2 to Dph7, in yeast and mammals. Here we show that diphthamide modification of eEF2 is conserved inArabidopsis thalianaand requires AtDPH1. Ribosomal \uffe2\uff88\uff921 frameshifting-error rates are increased in Arabidopsisdph1mutants, similar to yeast and mice. Compared to the wild type, shorter roots and smaller rosettes ofdph1mutants result from fewer formed cells. TARGET OF RAPAMYCIN (TOR) kinase activity is attenuated, and autophagy is activated, indph1mutants. Under abiotic stress diphthamide-unmodified eEF2 accumulates in wild-type seedlings, most strongly upon heavy metal excess, which is conserved in human cells. In summary, our results suggest that diphthamide contributes to the functionality of the translational machinery monitored by plants to regulate growth. Natural nitrogen isotopic signature reveals deprotonation during ammonium transport across living organisms.
The repurposing of by-products and the reduction of waste from food processing streams is an ever-increasing area of interest. Brewer\uffe2\uff80\uff99s spent yeast (BSY) is a prevalent by-product of the brewing industry. The spent yeast cells are removed at the end of the bulk fermentation. A small amount of it is used to start the next batch of fermentation; however, the majority of the spent yeast is discarded. This discarded yeast is high in nutrients, in particular proteins, vitamins and minerals, as well as containing functional and biologically active compounds such as polyphenols, antioxidants, \uffce\uffb2-glucans and mannoproteins. At present, BSY is mainly used in animal feed as a cheap and readily available source of protein. This review explores alternative, value-added applications for brewer\uffe2\uff80\uff99s spent yeast including nutritional ingredients, functional food additives as well as non-food applications. A major challenge in the utilization of BSY in food for human consumption is the high level of RNA. An excess of RNA in the diet can lead to an increase in uric acid in the bloodstream, potentially causing painful health conditions like gout. This issue can be overcome by RNA degradation and removal via additional treatment, namely heat treatment and enzymatic treatment. There is potential for the use of BSY ingredients in various food applications, including meat substitutes, bakery products and savory snacks.
", "keywords": ["2. Zero hunger", "TP500-660", "Brewer\u2019s yeast", "Fermentation industries. Beverages. Alcohol", "Saccharomyces cerevisiae", "04 agricultural and veterinary sciences", "brewer\u2019s yeast", "7. Clean energy", "yeast \u03b2-glucans", "12. Responsible consumption", "0404 agricultural biotechnology", "Fermentation", "Food applications", "saccharomyces cerevisiae", "Yeast \u03b2-glucans", "food applications", "fermentation"]}, "links": [{"href": "https://www.mdpi.com/2311-5637/6/4/123/pdf"}, {"href": "https://doi.org/10.3390/fermentation6040123"}, {"rel": "related", "href": "https://repository.soilwise-he.eu/cat/collections/metadata:main/items/Fermentation", "name": "related record", "description": "related record", "type": "application/json"}, {"rel": "self", "type": "application/geo+json", "title": "10.3390/fermentation6040123", "name": "item", "description": "10.3390/fermentation6040123", "href": "https://repository.soilwise-he.eu/cat/collections/metadata:main/items/10.3390/fermentation6040123"}, {"rel": "collection", "type": "application/json", "title": "Collection", "name": "collection", "description": "Collection", "href": "https://repository.soilwise-he.eu/cat/collections/metadata:main"}], "time": {"date": "2020-12-11T00:00:00Z"}}, {"id": "10115/29781", "type": "Feature", "geometry": null, "properties": {"updated": "2026-06-24T16:25:26Z", "type": "Journal Article", "created": "2022-07-11", "title": "Translational fidelity and growth of Arabidopsis require stress-sensitive diphthamide biosynthesis", "description": "AbstractDiphthamide, a post-translationally modified histidine residue of eukaryotic TRANSLATION ELONGATION FACTOR2 (eEF2), is the human host cell-sensitizing target of diphtheria toxin. Diphthamide biosynthesis depends on the 4Fe-4S-cluster protein Dph1 catalyzing the first committed step, as well as Dph2 to Dph7, in yeast and mammals. Here we show that diphthamide modification of eEF2 is conserved inArabidopsis thalianaand requires AtDPH1. Ribosomal \uffe2\uff88\uff921 frameshifting-error rates are increased in Arabidopsisdph1mutants, similar to yeast and mice. Compared to the wild type, shorter roots and smaller rosettes ofdph1mutants result from fewer formed cells. TARGET OF RAPAMYCIN (TOR) kinase activity is attenuated, and autophagy is activated, indph1mutants. Under abiotic stress diphthamide-unmodified eEF2 accumulates in wild-type seedlings, most strongly upon heavy metal excess, which is conserved in human cells. In summary, our results suggest that diphthamide contributes to the functionality of the translational machinery monitored by plants to regulate growth. Natural nitrogen isotopic signature reveals deprotonation during ammonium transport across living organisms.