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  • 1
    Electronic Resource
    Electronic Resource
    s.l. : American Chemical Society
    Biochemistry 25 (1986), S. 2027-2032 
    ISSN: 1520-4995
    Source: ACS Legacy Archives
    Topics: Biology , Chemistry and Pharmacology
    Type of Medium: Electronic Resource
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  • 2
    Electronic Resource
    Electronic Resource
    Copenhagen : Munksgaard International Publishers
    Physiologia plantarum 104 (1998), S. 0 
    ISSN: 1399-3054
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology
    Notes: In recent years, the analysis of hydrolytic enzyme gene expression in germinating cereals has progressed from a determination of hormone-responsive promoter elements to the cloning of positive and negative promoter-binding proteins and the direct in vivo demonstration of their effects on gene expression. Interesting parallels with animal systems have emerged, particularly with regard to the mediation of gibberellin signal transduction through transcriptional regulators encoded by oncogene homologues, calcium signalling pathways, and (possibly) through the phospho-inositide turnover pathway. New applications of cell microinjection, intracellular fluorescent probes and transient expression with effector/reporter expression plasmids have allowed direct examination of the roles of signal transduction factors and their ultimate targets of their pathways on hormone- and sugar-responsive gene promoter elements. Arabidopsis hormone response mutants have provided cloned candidates for genes encoding trans-acting regulatory proteins, and these have rapidly led to their counterparts in cereals. The identification of the initial receptor for gibberellin and abscisic acid still proves to be an intractable problem, but candidates have emerged from recent studies. The puzzle of how gibberellin and abscisic acid signal transductions lead to opposing regulatory events at every level proves to be a continuing challenge, but recent studies provide intriguing insights into these complex events. These studies are providing testable models as to how hydrolytic enzyme gene expression in developing and germinating cereal grains is regulated. The following review is constructed to summarize recent physiological, genetic and molecular studies in these areas and, where appropriate, provide correlative information from past studies.
    Type of Medium: Electronic Resource
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  • 3
    Electronic Resource
    Electronic Resource
    Oxford, UK : Blackwell Publishing Ltd
    Physiologia plantarum 96 (1996), S. 0 
    ISSN: 1399-3054
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology
    Notes: Cloned catalase probes from barley (Hordeum vulgare L.) and maize (Zea mays L.) were used to examine catalase gene expression in greened and etiolated leaves of several barley lines. Etiolated leaves had greater levels of an mRNA detected by barley Cat1, compared with greened leaves, in all lines. In contrast, a Cat2-like mRNA (homologous to Cat2 of maize) was induced by light and accumulated to high levels in greened leaves, compared to the negligible levels detected in etiolated leaves. This suggests that barley contains light-inducible and light-repressible catalase genes. In the catalase-deficient barley mutant RPr 79/4, no hybridization signal was detected when RNA from greened or etiolated leaves was probed with maize Cat2, indicating that this mutant is deficient for the light-induced Cat mRNA. In etiolated seedlings of both RPr 79/4 and its motherline, the level of the Cat1 mRNA increased coordinately with a steady increase in catalase activity. Even though the mutant RPr 79/4 was able to grow to maturity in normal air, it sustained chlorosis and significant head sterility, probably due to the lack of a light-inducible catalase. Although the mutant RPr 79/4 is not completely lacking catalase (EC 1.11.1.6), the loss of the CAT-1 isozyme is evidently harmful. This observation underscores the protective role of catalases in plants.
    Type of Medium: Electronic Resource
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  • 4
    Electronic Resource
    Electronic Resource
    Springer
    Plant molecular biology 29 (1995), S. 1005-1014 
    ISSN: 1573-5028
    Keywords: evolution ; genome mapping ; isozymes ; oxygen radicals ; powdery mildew
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract Clones representing two distinct barley catalase genes, Cat1 and Cat2, were found in a cDNA library prepared from seedling polysomal mRNA. Both clones were sequenced, and their deduced amino acid sequences were found to have high homology with maize and rice catalase genes. Cat1 had a 91% deduced amino acid sequence identity to CAT-1 of maize and 92% to CAT B of rice. Cat2 had 72 and 79% amino acid sequence identities to maize CAT-2 and-3 and 89% to CAT A of rice. Barley, maize or rice isozymes could be divided into two distinct groups by amino acid homologies, with one group homologous to the mitochondria-associated CAT-3 of maize and the other homologous to the maize peroxisomal/glyoxysomal CAT-1. Both barley CATs contained possible peroxisomal targeting signals, but neither had favorable mitochondrial targeting sequences. Cat1 mRNA occurred in whole endosperms (aleurones plus starchy endosperm), in isolated aleurones and in developing seeds, but Cat2 mRNA was virtually absent. Both mRNAs displayed different developmental expression patterns in scutella of germinating seeds. Cat2 mRNA predominated in etiolated seedling shoots and leaf blades. Barley genomic DNA contained two genes for Cat1 and one gene for Cat2. The Cat2 gene was mapped to the long arm of chromosome 4, 2.9 cM in telomeric orientation from the mlo locus conferring resistance to the powdery mildew fungus (Erysiphe graminis f.sp. hordei).
    Type of Medium: Electronic Resource
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  • 5
    Electronic Resource
    Electronic Resource
    Springer
    Plant molecular biology 30 (1996), S. 229-241 
    ISSN: 1573-5028
    Keywords: α-amylase ; barley ; GA ; gene-expression ; α-glucosidase ; maltase
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract A putative α-glucosidase clone has been isolated from a cDNA library constructed from mRNA of barley aleurones treated with gibberellin A3 (GA). The clone is 2752 bp in length and has an uninterrupted open reading frame encoding a polypeptide of 877 amino acids. A 680 amino acid region is 43% identical to human lysosomal α-glucosidase and other glycosyl hydrolases. In isolated aleurones, the levels of the corresponding mRNA increase strongly after the application of GA, similar to the pattern exhibited by low-pI α-amylase mRNA. High levels are also observed in the aleurone and scutellum after germination, while low levels are found in developing seeds. The genome contains a single form of this α-glucosidase gene and two additional sequences that may be related genes or pseudogenes.
    Type of Medium: Electronic Resource
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  • 6
    ISSN: 1573-5028
    Keywords: germination ; heterologous expression ; maltase ; Pichia ; recombinant protein ; starch hydrolysis
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract An α-glucosidase cDNA clone derived from barley aleurone tissue was expressed in Pichia pastoris and Escherichia coli. The gene was fused with the N-terminal region of the Saccharomyces cerevisiae α-factor secretory peptide and placed under control of the Pichia AOX1 promoter in the vector pPIC9. Enzymatically active, recombinant α-glucosidase was synthesized and secreted from the yeast upon induction with methanol. The enzyme hydrolyzed maltose 〉 trehalose 〉 nigerose 〉 isomaltose. Maltase activity occurred over the pH range 3.5–6.3 with an optimum at pH 4.3, classifying the enzyme as an acid α-glucosidase. The enzyme had a Km of 1.88 mM and Vmax of 0.054 µmol/min on maltose. The recombinant α-glucosidase expressed in E. coli was used to generate polyclonal antibodies. The antibodies detected 101 and 95 kDa forms of barley α-glucosidase early in seed germination. Their levels declined sharply later in germination, as an 81 kDa α-glucosidase became prominent. Synthesis of these proteins also occurred in isolated aleurones after treatment with gibberellin, and this was accompanied by a 14-fold increase in α-glucosidase enzyme activity. Abbreviations: AGL, barley seed α-glucosidase; rAGL, recombinant barley seed α-glucosidase; BMGY, buffered glycerol-complex medium; BMMY, buffered methanol-complex medium; GA, gibberellic acid; UTR, untranslated region.
    Type of Medium: Electronic Resource
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  • 7
    Electronic Resource
    Electronic Resource
    Chichester [u.a.] : Wiley-Blackwell
    Developmental Genetics 10 (1989), S. 1-10 
    ISSN: 0192-253X
    Keywords: Glyoxysomes ; CAT-2 ; Scutella ; Rocket immunoelectrophoresis ; Life and Medical Sciences ; Genetics
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Notes: Previous studies showed that the expression of catalase-2 (CAT-2) and other glyoxysomal proteins is independently controlled in the scutella of intact maize seedlings. In this study, removal of the embryonic axis prior to seed imbibition dramatically decreased the amounts of all but two of the 19 immunologically detectable glyoxysomal proteins in the scutellum, including CAT-2. The temporal expression profile of CAT-2 was also altered. Removal of the axis after seeds were fully imbibed (24 hr) had little effect on the subsequent pattern of expression of CAT-2. The effect of axis removal was specific for glyoxysomal enzymes and caused relatively little change in the population of stainable scutellar proteins. In vitro translation studies and nucleic acid hybridization with a gene-specific cloned probe (for Cat2) revealed that the mRNA levels for glyoxysomal proteins were sharply lowered by axis removal. This study provides evidence that a signal may be released from the embryonic axis during imbibition, leading to the expression of a set of glyoxysomal enzymes by enhancing either the transcription of their genes or transcript stability.
    Additional Material: 8 Ill.
    Type of Medium: Electronic Resource
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  • 8
    Electronic Resource
    Electronic Resource
    Chichester [u.a.] : Wiley-Blackwell
    Developmental Genetics 11 (1990), S. 280-288 
    ISSN: 0192-253X
    Keywords: Seed germination ; transcription control ; compartmentalization ; polysomes ; Life and Medical Sciences ; Genetics
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Notes: The temporal expression pattern of the CAT-2 catalase isozyme in scutella of Zea mays seedlings normally coincides with that of other major glyoxysomal enzymes. In standard genetic lines (e.g., W64A), the CAT-2 enzyme is synthesized de novo after imbibition, reaches a peak at approximately 4 days later, and then declines steadily. In a high CAT-2 genetic line, R6-67, the enzyme accumulates in a linear fashion for at least 8 days after imbibition and reaches a level 3-fold higher than in W64A. During the first 9 days of early seedling growth in W64A, the correlation between Cat2 mRNA levels and CAT-2 protein suggests that pretranslational control governs Cat2 gene expression. In R6-67, the steady rise in CAT-2 protein appears to result from a pretranslational control mechanism in which Cat-2 mRNA apparently never declines to levels which would limit the rate of accumulation of CAT-2 protein. In addition, the amount of Cat2 mRNA bound to polysomes is 3-fold higher in R6-67 at day 9 relative to W64A at day 9, reflecting a much greater capacity to synthesize CAT-2 later in development. Despite substantial differences in Cat2 mRNA levels between genetic lines, early CAT-2 protein accumulation is similar until day 5, when other glyoxysomal enzymes also attain maximal activity levels. The early increase in CAT-2, between day 2 and day 5 post-imbibition, occurs despite a sharp decline in polysomal Cat2 mRNA. This is related to a transient decline in total extractable polysomes which paradoxically coincides with the peak in glyoxysomal enzyme activities. Early Cat2 gene expression is likely controlled by the compartmentalization of CAT-2 in glyoxysomes.
    Additional Material: 8 Ill.
    Type of Medium: Electronic Resource
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