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  • Protein (abscisic acid-responsive)  (2)
  • PROPELLANTS  (1)
  • Stress-inducible protein  (1)
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  • 1
    Digitale Medien
    Digitale Medien
    Springer
    Planta 191 (1993), S. 7-17 
    ISSN: 1432-2048
    Schlagwort(e): Abscisic acid ; Developmental regulation ; Pathogenesis-related protein ; Pisum ; Protein (abscisic acid-responsive) ; Stress-inducible protein ; Tissue-specific protein
    Quelle: Springer Online Journal Archives 1860-2000
    Thema: Biologie
    Notizen: Abstract The expression of members of two closely related abscisic acid (ABA)-responsive pea protein families, ABR17 and ABR18 (ABA-responsive 17200-Mr and 18100-Mr, respectively), is developmentally, tissueand stress-specifically regulated. Two-dimensional polyacrylamide gel electrophoresis revealed a number of ABR polypeptides on fluorographs of immunoprecipitated translation products of mRNAs, depending on the tissue, stage of development or type of stress. High endogenous ABA, or added ABA, enhanced the accumulation of translatable mRNA for specific ABR members under certain conditions, but high endogenous ABA was not a pre-requisite for accumulation of translatable ABR mRNA. The accumulation of ABR polypeptides was examined by Western blot analysis of acetate-buffer-extracted proteins. In fully expanded, young unstressed leaves, the ABR17 polypeptides (ABR18 polypeptides not detectable) accumulated to markedly higher levels in the epidermis than in the mesophyll. Dehydration stress caused an increased (ABR17) and detectable (ABR18) polypeptide accumulation which occurred predominantly in the epidermis. Detached leaves were used further to characterise factors affecting ABR polypeptide accumulation. An enhanced (ABR17) and detectable (ABR18) polypeptide accumulation occurred in the presence of ABA (10−4 M) but ABR18-polypeptide accumulation required light. The accumulation of both ABR polypeptides was stimulated in the presence of metabolisable and non-metabolisable carbohydrate sources but not in water or glutamine, indicating an osmotic rather than metabolic response. This carbohydrate-stimulated accumulation was markedly enhanced by light but unaffected by 3-(3,4-dichlorophenyl)-1,1-dimethylurea, an inhibitor of photosynthesis, indicating other photoreceptive processes besides photosynthesis were involved. The function of the ABR proteins remains unknown but their accumulation in aging tissues indicates a role in senescence. The results clearly demonstrate highly complex interactions between different environmental and developmental signals leading to the expression of these stressrelated proteins. In light of these results, the induction of protein expression of the newly-termed intracellular pathogenesis-related proteins, to which the ABR proteins are closely related, is discussed.
    Materialart: Digitale Medien
    Standort Signatur Erwartet Verfügbarkeit
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  • 2
    Digitale Medien
    Digitale Medien
    Springer
    Planta 184 (1991), S. 14-23 
    ISSN: 1432-2048
    Schlagwort(e): Abscisic acid ; Late embryogenesis abundant proteins ; Pathogenesis-related protein ; Pisum (embryogenesis) ; Protein (abscisic acid-responsive) ; Seed development
    Quelle: Springer Online Journal Archives 1860-2000
    Thema: Biologie
    Notizen: Abstract Two abscisic acid (ABA)-responsive seed proteins, ABR17 and ABR18 (ABA-responsive 17000-Mr and 18000-Mr, respectively), previously found to be induced in cultured embryos of pea (Pisum sativum L.) are major components synthesised during normal seed desiccation. The ABR17 and ABR18 proteins showed different patterns of accumulation. The ABR18 protein was abundant in the testa during early seed development but in desiccating seed it was synthesised in the embryo, indicating spacial as well as temporal regulation of expression. The ABR18 protein was undetectable soon after germination but reappeared after adding ABA. The ABR17 protein was not detected in the testa but appeared in the embryo just prior to maximum fresh weight. The ABR17 protein continued to be synthesised during germination and was also present in non-stressed leaves. A high level of endogenous ABA or added ABA increased levels of translatable ABR17 mRNA. The ABR17 and ABR18 proteins were further characterised so as to help determine their structure and function. Neither protein appeared to contain a signal peptide but both proteins appeared to be glycosylated. The proteins had similar amino-acid compositions and limited Nterminal analysis showed 56% sequence identity. Neither protein had any significant N-terminal sequence homology to any of the late embryogenesis-abundant (LEA) proteins or dehydrins. Both proteins, however, show striking homology with a pea disease-resistance-response protein and the major birch pollen allergen, indicating that the ABR17 and ABR18 proteins may be members of a distinct group of stress-induced proteins.
    Materialart: Digitale Medien
    Standort Signatur Erwartet Verfügbarkeit
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  • 3
    Publikationsdatum: 2019-05-10
    Beschreibung: Thermal decomposition of cesium hydride for in- flight fuel generation for a cesium ion engine
    Schlagwort(e): PROPELLANTS
    Format: text
    Standort Signatur Erwartet Verfügbarkeit
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