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  • Low temperature  (2)
  • Phospholipase A"2  (2)
  • 1
    Electronic Resource
    Electronic Resource
    Amsterdam : Elsevier
    Biochimica et Biophysica Acta (BBA)/Molecular Cell Research 1094 (1991), S. 161-167 
    ISSN: 0167-4889
    Keywords: Inositol triphosphate ; Phospholipase A"2 ; Phospholipase C ; Prostacyclin
    Source: Elsevier Journal Backfiles on ScienceDirect 1907 - 2002
    Topics: Biology , Chemistry and Pharmacology , Medicine , Physics
    Type of Medium: Electronic Resource
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  • 2
    Electronic Resource
    Electronic Resource
    Amsterdam : Elsevier
    Biochimica et Biophysica Acta (BBA)/Molecular Cell Research 1055 (1990), S. 223-229 
    ISSN: 0167-4889
    Keywords: Phospholipase A"2 ; Phospholipase C ; Prostacyclin synthesis ; Streptokinase
    Source: Elsevier Journal Backfiles on ScienceDirect 1907 - 2002
    Topics: Biology , Chemistry and Pharmacology , Medicine , Physics
    Type of Medium: Electronic Resource
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  • 3
    Electronic Resource
    Electronic Resource
    Springer
    Molecular genetics and genomics 262 (1999), S. 534-542 
    ISSN: 1617-4623
    Keywords: Key words MAP kinase ; Low temperature ; Senescence ; Maize ; cDNA cloning
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract Four species of protein kinase were identified in senescent maize leaves using a gel assay for kinase activity with myelin basic protein (MBP) as the substrate. Most of these kinases were also found in healthy green leaves that had been exposed to low-temperature stress (5° C) and then returned to 25° C. A 41-kDa protein was activated in senescent leaves, whereas a 45-kDa protein was activated 3 h after up-shift from 5° C to 25° C as well as in senescent leaves. A 39-kDa protein was activated by cold stress. The other two proteins, of 35 kDa and 52 kDa, constitutively phosphorylated MBP during senescence and temperature up-shift. Judging from their molecular masses, cation requirements and substrate specificities, it seemed likely that the 39-kDa, 41-kDa and 45-kDa proteins represented mitogen-activated protein kinases (MAPKs). Subsequently two MAPK cDNAs were isolated from a cDNA library constructed using mRNAs from senescent leaves. Northern analysis showed that the transcript corresponding to one of the cDNAs, designated ZmMPK5, accumulated in healthy leaves 3 h after the up-shift to 25° C as well as in senescent leaves, suggesting that the 45-kDa protein kinase is encoded by ZmMPK5. Western analysis using an antiserum against the C-terminal region of ZmMPK5 showed that the level of the ZmMPK5 protein increased in senescent leaves. These results indicate that a 45-kDa MAPK is involved in the process of senescence and in recovery from low-temperature stress in maize plants.
    Type of Medium: Electronic Resource
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  • 4
    ISSN: 1617-4623
    Keywords: Key words Cytokinins ; Low temperature ; Oryza sativa ; Protein kinase ; Zea mays
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract The wheat gene WPK4 encodes a 56-kDa protein kinase that belongs to group 3 of the SNF1-related protein kinase family (SnRK3), and is up-regulated by light and cytokinins and down-regulated by sucrose. In order to determine whether or not this particular regulation pattern is general among plant species, we isolated and characterized homologous genes from rice and maize. Two rice genes, OsPK4 and OsPK7, encode proteins comprising 508 and 520 amino acids, and show, respectively, 75% and 76% sequence similarity to WPK4. OsPK4 and OsPK7 proteins produced in Escherichia coli were able to phosphorylate themselves and myelin basic proteins, the reaction requiring magnesium and/or manganese ions. Transcripts of OsPK4 were detected in all tissues tested, and amounts were increased upon illumination, nutrient deprivation and treatment with cytokinins. In contrast, transcripts of OsPK7 were not found in any tissues except in mature leaves at low levels, and did not accumulate under any of the stress conditions examined. A maize gene, ZmPK4, encodes a protein with 518 amino acids that shows 74% similarity to WPK4. Its transcripts were constitutively expressed in all tissues, regardless of light, nutrient and cytokinin status, but were increased upon exposure to low temperature. These results indicate that, despite the sequence similarity between their products, genes for SnRK3 proteins are differentially regulated in response to environmental stimuli.
    Type of Medium: Electronic Resource
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