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  • 1
    Electronic Resource
    Electronic Resource
    Comparative properties of genetically defined peptidases in maize (1980)
    s.l. : American Chemical Society
    Biochemistry 19 (1980), S. 4660-4667 
    Details
    ISSN: 1520-4995
    Source: ACS Legacy Archives
    Topics: Biology , Chemistry and Pharmacology
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1021/bi00561a019
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  • 2
    Electronic Resource
    Electronic Resource
    Evidence for the processing of maize catalase-2 and purification of its messenger RNA aided by translation of antibody-bound polysomes (1986)
    s.l. : American Chemical Society
    Biochemistry 25 (1986), S. 2027-2032 
    Details
    ISSN: 1520-4995
    Source: ACS Legacy Archives
    Topics: Biology , Chemistry and Pharmacology
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1021/bi00356a029
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  • 3
    Electronic Resource
    Electronic Resource
    GENETIC CONTROL OF MULTIPLE MOLECULAR FORMS OF CATALASE IN MAIZE (1968)
    Oxford, UK : Blackwell Publishing Ltd
    Annals of the New York Academy of Sciences 151 (1968), S. 0 
    Details
    ISSN: 1749-6632
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Natural Sciences in General
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1749-6632.1968.tb11896.x
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  • 4
    Electronic Resource
    Electronic Resource
    Effects of the plant growth regulator abscisic acid and high osmoticum on the developmental expression of the maize catalase genes (1998)
    Copenhagen : Munksgaard International Publishers
    Physiologia plantarum 104 (1998), S. 0 
    Details
    ISSN: 1399-3054
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology
    Notes: The effects of abscisic acid (ABA) and high osmoticum on catalase (Cat) gene expression in maize have been examined. Each Cat gene responds differently to ABA and osmotic stress at different developmental stages and in different tissues. Cat1 transcript accumulates to high levels in developing and germinating embryos, and in leaves. In embryos, Cat2 and Cat3 transcripts are up-regulated only at very high ABA concentrations during late embryogenesis and in response to various concentrations of ABA in germinating embryos. Cat3 transcript is down-regulated by ABA and osmotic stress in leaves. Accumulation of Cat1 transcript in response to osmotic stress is a consequence of increased endogenous ABA levels. Our data suggest that two separate pathways might be involved in the ABA-mediated induction of Cat1. The Vp1 trans-acting factor is required for maximum induction of Cat1 transcript in wild-type (Vp1/—) and in W64A developing embryos; however, Vp1 is not required for inducing the Cat1 transcript in vp1 mutant developing embryos, nor in W64A germinating embryos or in leaves. Given the fact that the Cat genes have a known function, we hypothesize that the increase in Cat gene products in response to ABA is due, in part, to ABA-mediated metabolic changes leading to changes in oxygen free radical levels, which in turn, lead to the induction of the antioxidant defense system.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1034/j.1399-3054.1998.1040317.x
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  • 5
    Electronic Resource
    Electronic Resource
    Two barley catalase genes respond differentially to light (1996)
    Oxford, UK : Blackwell Publishing Ltd
    Physiologia plantarum 96 (1996), S. 0 
    Details
    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
    URL: http://dx.doi.org/10.1111/j.1399-3054.1996.tb00446.x
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  • 6
    Electronic Resource
    Electronic Resource
    Response of the maize catalases and superoxide dismutases to cercosporin-containing fungal extracts: the pattern of catalase response in scutella is stage specific (1993)
    Oxford, UK : Blackwell Publishing Ltd
    Physiologia plantarum 88 (1993), S. 0 
    Details
    ISSN: 1399-3054
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology
    Notes: Cercosporin, a photoactivated polyketide toxin produced by fungi of the genus Cercospora, reacts with molecular oxygen to produce oxygen radicals. Using both minus-and plus-cercosporin fungal extracts and purified cercosporin, we have analyzed antioxdant defense gene responses in maize scutella at two stages in development. The three maize catalases (CATH2O2: H2O2 oxidoreductase, EC 1.11.1.6) respond differentially to applied cercosporin, and this response varies with developmental stage. Total catalase activity, as well as individual isozyme proteins and their corresponding steady-state levels of RNA changed in parallel in response to applied cercosporin. In contrast, both toal superoxide dismutase (SOD, O2:O2 oxidoreductase; EC 1.15.1.1) activity and individual isozyme protein levels remained constant in all treatments. Sod transcript accumulation, however, changed dramatically. Comparison of the response of these genes to minus- and plus-cercosporin fungal extracts with their response to purified cercosporin demonstrated that other fungal compounds influence the expression of bothSod and Cat.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1399-3054.1993.tb01773.x
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  • 7
    Electronic Resource
    Electronic Resource
    Spatial and temporal responses of the maize catalases to low temperature (1997)
    Oxford, UK : Blackwell Publishing Ltd
    Physiologia plantarum 101 (1997), S. 0 
    Details
    ISSN: 1399-3054
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology
    Notes: Catalase (H2O2:H2O2 oxidoreductase, EC 1.11.1.6) is a primary antioxidant enzyme that can remove H2H2 rapidly and prevent the formation of reactive oxygen species. The maize (Zea mays L.) catalase genes are regulated in their expression spatially and temporally. Using embryos from germinating seeds and developing kernels from the maize standard inbred line W64A, which expresses all three Cat genes, and the CAT-2 null line A338F, we have examined the response of the three catalase genes to low temperatures (14°C, 4°C, or 14/4°C). Total catalase activity increased in response to low temperatures in germinating embryos of both maize lines. Zymogram analysis showed that the increase in total catalase activity was due to accumulation of the CAT-1 and CAT-2 isozymes in the scutella and embryonic axes of germinating embryos. In both lines, CAT-3 activity decreased in the embryonic axes of germinating embryos in response to low temperatures. The steady-state levels of Cat transcripts did not parallel the pattern of the corresponding catalase proteins, indicating the involvement of post-transcriptional control mechanisms. In contrast to germinating embryos and excepting an increase at 4°C in A338F, total catalase activity decreased in response to low temperatures in scutella of developing embryos of both lines. CAT-2 activity (in W64A) and CAT-3 activity (in A338F) decreased in response to low temperatures and their corresponding steady-state levels of mRNA also decreased. Only CAT-1 activity increased dramatically at 4°C in A338F, but Cat I transcript level did not change. Our data indicate that the three maize catalase genes respond differentially to low temperatures at two different developmental stages.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1399-3054.1997.tb01831.x
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  • 8
    Electronic Resource
    Electronic Resource
    Molecular biology of intracellular protein trafficking (1988)
    Oxford, UK : Blackwell Publishing Ltd
    Physiologia plantarum 74 (1988), S. 0 
    Details
    ISSN: 1399-3054
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology
    Notes: The evidence accumulated to date indicates that protein compartmentalization is mediated through specific regions of proteins destined for translocation into subcellular organelles. Proteins targeted to mitochondria, chloroplasts or the endoplasmic reticulum have ‘transit’ sequences contained in amino-terminal peptide extensions. However, most peroxisomal proteins do not have amino-terminal extensions. Protein importation into mitochondria has been extensively studied and characterized. This post-translational process appears to involve receptors on the mitochondrial outer membrane, and is dependent upon the electrochemical gradient across the inner membrane. Translocation to one of the submitochondrial compartments is determined by the type of transit sequence contained in a mitochondrial protein. The majority of imported mitochondrial proteins are proteolytically altered prior to assembly into oligomeric enzyme complexes. Protein importation into peroxisomes is distinctly different from importation into mitochondria. Although both processes are post-translational, their only other similarity is a requirement for ATP. In this review, we present and compare recent evidence for both mitochondrial and peroxisomal protein importation.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1399-3054.1988.tb00649.x
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  • 9
    Electronic Resource
    Electronic Resource
    Role of hydrogen peroxide and different classes of antioxidants in the regulation of catalase and glutathione S-transferase gene expression in maize (Zea mays L.) (1999)
    Copenhagen : Munksgaard
    Physiologia plantarum 106 (1999), S. 0 
    Details
    ISSN: 1399-3054
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology
    Notes: The role of hydrogen peroxide (H2O2) and various antioxidants in the regulation of expression of the three Cat and Gst1 genes of maize (Zea mays L.) has been investigated. Low concentrations of H2O2 appeared to inhibit Cat1, Cat3, and Gst1 gene expression, while higher doses strongly induced these genes. Time course experiments indicated that high concentrations of H2O2 induced Cat1, Cat2, and Gst1 gene expression to higher levels, and in less time, than lower H2O2 concentrations. Induction of Cat3 was superimposed on the circadian regulation of the gene. These results demonstrate a direct signaling action of H2O2 in the regulation of antioxidant gene responses in maize.The effects of the antioxidant compounds N-acetylcysteine, pyrrolidine dithiocarbamate, hydroquinone, and the electrophile antioxidant responsive element (ARE)-inducer β-naphthoflavone were quite different and specific for each gene/compound/concentration combination examined. The response of each gene to each antioxidant compound tested was unique, suggesting that the ability of these compounds to affect expression of the maize Cat and Gst1 genes may not be the result of a common (antioxidant) mode of action. A putative regulatory ARE motif involved in the regulation of antioxidant and oxidative stress gene responses in mammalian systems is present in the promoter of all three maize catalase genes and we tested its ability to interact with nuclear extracts prepared from 10 days post-imbibition senescing scutella. Protein-DNA interactions in the ARE motif and the U2 snRNA homologous regions of the Cat1 promoter were observed, suggesting that ARE may play a role in the high induction of Cat1 in a tissue which, due to senescence, is under oxidative stress.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1034/j.1399-3054.1999.106116.x
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  • 10
    Electronic Resource
    Electronic Resource
    Catalase gene expression in response to auxin-mediated developmental signals (2002)
    Oxford, UK : Blackwell Science, Ltd
    Physiologia plantarum 114 (2002), S. 0 
    Details
    ISSN: 1399-3054
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology
    Notes: The effect of auxin on maize catalase gene expression was examined at several different developmental stages during embryo and seedling development. All three catalase genes and their respective proteins were induced by both natural and synthetic auxin in immature embryos. Total catalase (CAT) activity increased dramatically in response to high concentrations of auxin, with CAT-2, which is not normally expressed at this stage, being the isozyme most responsible for the increase. Cat1 transcript accumulated to high levels at 2–8 h after auxin treatment, while Cat2 and Cat3 transcripts increased dramatically, but only after 12 h. In CAT-2 null mutant lines, the CAT-1 isozyme compensated for the missing CAT-2 activity and was the major isozyme responsible for the observed increase in total CAT activity. Auxin treatment mimics the germination process (i.e. induces germination) in immature embryos. Thus, the observed early induction of CAT-1 and the later increase of CAT-2 during the germination process may be due, in part, to changes in auxin content. In germinating embryos, auxin also induces total CAT activity and Cat transcript accumulation, although to a lesser extent. Auxin also induces Cat1 transcript accumulation in young leaves. The involvement of ROS in the auxin response is discussed.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1034/j.1399-3054.2002.1140215.x
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