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  • Arabidopsis thaliana  (2)
  • Jasmonic acid  (2)
  • 1
    Electronic Resource
    Electronic Resource
    Aspirin prevents wound-induced gene expression in tomato leaves by blocking jasmonic acid biosynthesis (1993)
    Springer
    Planta 191 (1993), S. 123-128 
    Details
    ISSN: 1432-2048
    Keywords: Aspirin ; Gene expression ; Jasmonic acid ; Lycopersicon ; Proteinase inhibitor II ; Wounding
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract Jasmonic acid (JA) and its methyl ester, like mechanical wounding, strongly induce accumulation of proteinase inhibitor II (Pin2) in tomato and potato leaves. In plants, JA is synthesized from α-linolenic acid by a lipoxygenase (LOX)-mediated oxygenation leading to 13-hydroxyperoxylinolenic acid (13-HPLA) which is then subsequently transformed to JA by the action of hydroperoxide-dehydrase activity and additional modification steps. Both the chemical structure as well as the biosynthetic pathway of JA resemble those of the mammalian eicosanoids (prostaglandins and leukotrienes) which are derived from LOX-and cyclooxygenase (COX)-mediated reactions. To assess the role of endogenous JA in the wound response, detached tomato (Lycopersicon esculentum Mill.) leaves were supplied with different LOX and COX inhibitors and the expression of the wound-induced genes for Pin2 (Pin2), cathepsin D inhibitor (Cdi) and threonine deaminase (Td) was analyzed. Lipoxygenase inhibitors as well as some COX inhibitors blocked the wound-induced accumulation of Pin2, Cdi and Td mRNA. Quantitation of endogenous levels of JA showed that aspirin blocks the increase of this phytohormone normally observed as a result of wounding. Linolenic acid and 13-HPLA do not induce the expression of Pin2, Cdi and Td in the presence of aspirin. However, 12-oxo-phytodienoic acid and jasmonic acid are able to overcome the inhibitory effect of this substance. These results strongly indicate that aspirin prevents wound-induced gene activation by inhibiting the hydroxyperoxide-dehydrase activity that mediates the conversion of 13-HPLA to 12-oxo-phytodienoic acid.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00240903
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  • 2
    Electronic Resource
    Electronic Resource
    Methyljasmonate and α-linolenic acid are potent inducers of tendril coiling (1991)
    Springer
    Planta 185 (1991), S. 316-322 
    Details
    ISSN: 1432-2048
    Keywords: Bryonia ; Jasmonic acid ; Methyljasmonate ; α-Linolenic acid ; Tendril coiling
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract A coiling-inducing factor was isolated from tendrils of Bryonia dioica Jacq. and identified by infrared, 1H-, 13C-nuclear magnetic resonance and mass spectrometry as α-linolenic acid. When applied to detached tendrils, exogenous α-linolenic acid, but not linoleic acid or oleic acid, induced tendril coiling. Further investigations showed that metabolites of α-linolenic acid, jasmonic acid and, even more so, methyljasmonate, are highly effective inducers of tendril coiling in B. dioica. Methyljasmonate was most active when administered by air and, in atmospheric concentrations as low as 40–80 nM, induced a full free-coiling response with kinetics similar to mechanical stimulation. Even atmospheric levels as low as 4–5 nM methyljasmonate were still found to be significantly active. Methyljasmonate could be one of the endogenous chemical signals produced in mechanically stimulated parts of a tendril and, being highly volatile, act as a diffusible gaseous mediator spreading through the intracellular spaces to trigger free coiling of tendrils.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00201050
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  • 3
    Electronic Resource
    Electronic Resource
    Functional expression and molecular characterization of AtUBC2-1, a novel ubiquitin-conjugating enzyme (E2) from Arabidopsis thaliana (1993)
    Springer
    Plant molecular biology 23 (1993), S. 387-396 
    Details
    ISSN: 1573-5028
    Keywords: Arabidopsis thaliana ; ubiquitin carrier protein ; ubiquitin-conjugating enzyme ; ubiquitin-dependent proteolysis
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract The first member of a novel subfamily of ubiquitin-conjugating E2-proteins was cloned from a cDNA library of Arabidopsis thaliana. Genomic blots indicate that this gene family (AtUBC2) consists of two members and is distinct from AtUBC1, the only other E2 enzyme known from this species to date (M.L. Sullivan and R.D. Vierstra, Proc. Natl. Acad. Sci. USA 86 (1989) 9861-9865). The cDNA sequence of AtUBC2-1 extends over 794 bp which would encode a protein of 161 amino acids and a calculated molecular mass of 18.25 kDa. The protein encoded by AtUBC2-1 is shown to accept 125I-ubiquitin from wheat E1 enzymes, when expressed from Escherichia coli hosts as fusion protein carrying N-terminal extensions. It is deubiquitinated in the presence of lysine and, by these criteria, is considered a functional E2 enzyme.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00029013
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  • 4
    Electronic Resource
    Electronic Resource
    Cloning, molecular and functional characterization of Arabidopsis thaliana allene oxide synthase (CYP 74), the first enzyme of the octadecanoid pathway to jasmonates (1996)
    Springer
    Plant molecular biology 31 (1996), S. 323-335 
    Details
    ISSN: 1573-5028
    Keywords: Arabidopsis thaliana ; allene oxide synthase ; CYP74 ; octadecanoids ; jasmonate biosynthesis ; 12-oxo-phytodienoic acid
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract Allene oxide synthase, an enzyme of the octadecanoid pathway to jasmonates, was cloned from Arabidopsis thaliana as a full-length cDNA encoding a polypeptide of 517 amino acids with a calculated molecular mass of 58705 Da. From the sequence, an N-terminal transit peptide of 21 amino acids resembling chloroplast transit peptides was deduced. Three out of four invariant amino acid residues of cytochrome P450 heme-binding domains are conserved and properly positioned in the enzyme coding region, including the heme-accepting cysteine (Cys-470). Southern analysis indicated in A. thaliana only one allene oxide synthase gene to be present. While transcript levels were rapidly and transiently induced after wounding of the leaves, allene oxide synthase activity remained nearly constant at a low level of ca. 0.8 nkat per mg of protein. The cDNA encoding A. thaliana allene oxide synthase was highly expressed in bacteria giving rise to a polypeptide of the calculated molecular mass. The protein was enzymatically active, and verification of the reaction products by GC-MS showed that it was capable of utilizing not only 13-hydroperoxylinolenic acid (13-hydroperoxy-9(Z), 11(E), 15(Z)-octadecatrienoic acid), but also 13-hydroperoxylinoleic acid (13-hydroperoxy-9(Z), 11(E)-octadecadienoic acid) as substrate. The data suggest parallel pathways to jasmonates from linolenic acid or linoleic acid in A. thalina.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00021793
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