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  • Ethylene synthesis  (2)
  • 1-aminocyclopropane-1-carboxylate (ACC) synthase  (1)
  • Avena (ethylene synthesis)  (1)
  • 1
    ISSN: 1432-2048
    Keywords: d-Amino acid ; 1-Aminocyclopropane-1-carboxylic acid ; α-Aminoisobutyric acid ; Ethylene synthesis ; 1-(Malonylamino)cyclopropane-1-carboxylic acid ; α-(Malonylamino)isobutyric ; Vigna
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract 1-Aminocyclopropane-1-carboxylic acid (ACC) is known to be converted to ethylene and conjugated into N-malonyl-ACC in plant tissues. When α-amino[1-14C]isobutyric acid (AIB), a structural analog of ACC, was administered to mungbean (Vigna radiata L.) hypocotyl segments, it was metabolized to 14CO2 and conjugated to N-malonyl-AIB (MAIB). α-Aminoisobutyric acid inhibited the conversion of ACC to ethylene and also inhibited, to a lesser extent, N-malonylation of ACC and d-amino acids. Although the malonylation of AIB was strongly inhibited by ACC as well as by d-amino acids, the metabolism of AIB to CO2 was inhibited only by ACC but not by d-amino acids. Inhibitors of ACC conversion to ethylene such as anaerobiosis, 2,4-dinitrophenol and Co2+, similarly inhibited the conversion of AIB to CO2. These results indicate that the malonyalation of AIB to MAIB is intimately related to the malonylation of ACC and d-amino acids, whereas oxidative decarboxylation of AIB is related to the oxidative degradation of ACC to ethylene.
    Type of Medium: Electronic Resource
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  • 2
    ISSN: 1573-5028
    Keywords: 1-aminocyclopropane-1-carboxylate (ACC) synthase ; elicitor ; ethylene ; gene expression ; tomato
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract The key enzyme of ethylene biosynthesis, ACC synthase, is encoded by a multigene family. We describe three new DNA sequences encoding members of the ACC synthase family of the tomato. One of these sequences encodes a novel ACC synthase, LE-ACS6, which is phylogenetically related to the ACC synthases LE-ACS1A and LE-ACS1B. Gene-specific probes for seven tomato ACC synthase genes were prepared. They were used for RNase protection assays to study the accumulation of ACC synthase transcripts in suspension-cultured tomato cells after the addition of an elicitor. The ACC synthase genes LE-ACS2, LE-ACS5 and LE-ACS6 were strongly induced by the elicitor. In contrast, the genes LE-ACS1B, LE-ACS3 and LE-ACS4 were constitutively expressed and LE-ACS1B was present at all times at a particularly high level. Thus, there are two groups of ACC synthase transcripts expressed in these cells, either elicitor-induced or constitutive. A transcript of LE-ACS1A was not detected. Despite the presence of LE-ACS1B, LE-ACS2, LE-ACS3, LE-ACS4 and LE-ACS5, there was only little ethylene produced in the absence of the elicitor. Increased ethylene production is usually correlated with the accumulation of ACC synthase transcripts, indicating that ethylene production is controlled via the transcriptional activation of ACC synthase genes. However, the abundance of several ACC synthase mRNAs studied was not strictly correlated with the rate of elicitor-induced ethylene production. Our data provide evidence that the activity of these ACC synthases may not solely be controlled by the transcriptional activation of ACC synthase genes.
    Type of Medium: Electronic Resource
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  • 3
    ISSN: 1432-2048
    Keywords: 1-Aminocyclopropane-1-carboxylic acid ; Avena (ethylene synthesis) ; Lipoxygenase
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract In order to understand the physiological significance of the in-vitro lipoxygenase (EC 1.13.11.12)-mediated ethylene-forming system (J.F. Bousquet and K.V. Thimann 1984, Proc. Natl. Acad. Sci. USA 81, 1724–1727), its characteristics were compared to those of an in-vivo ethylene-forming system. While oat (Avena sativa L.) leaves, as other plant tissues, preferentially converted only one of the 1-amino-2-ethylcyclopropane-1-carboxylic acid (AEC) isomers to 1-butene, the lipoxygenase system converted all four AEC isomers to 1-butene with nearly equal efficiencies. While the in-vivo ethylene-forming system of oat leaves was saturable with ACC with a Km of 16 μM, the lipoxygenase system was not saturated with ACC even at 10 mM. In contrast to the in-vivo results, only 10% of the ACC consumed in the lipoxygenase system was converted to ethylene, indicating that the reaction is not specific for ethylene formation. Increased ACC-dependent ethylene production in oat leaves following pretreatment with linoleic acid has been inferred as evidence of the involvement of lipoxygenase in ethylene production. We found that pretreating oat leaves with linoleic acid resulted in increased ACC uptake and thereby increased ethylene production. A similar effect was observed with oleic acid, which is not a substrate of lipoxygenase. Since linoleic acid hydroperoxide can substitute for lipoxygenase and linoleic acid in this system, it is assumed that the alkoxy radicals generated during the decomposion of linoleic acid hydroperoxide are responsible for the degradation of ACC to ethylene. Our results collectively indicate that the reported lipoxygenase system is not the in-vivo ethylene-forming enzyme.
    Type of Medium: Electronic Resource
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  • 4
    ISSN: 1432-2048
    Keywords: 1-Amninocyclopropane-1-carboxylate synthase ; cDNA ; Ethylene synthesis ; Fruit ripening ; Gene expression ; Malus
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract 1-Aminocyclopropane-1-carboxylate (ACC) synthase (EC 4.4.1.14) purified from apple (Malus sylvestris Mill.) fruit was subjected to trypsin digestion. Following separation by reversed-phase high-pressure liquid chromatography, ten tryptic peptides were sequenced. Based on the sequences of three tryptic peptides, three sets of mixed oligonucleotide probes were synthesized and used to screen a plasmid cDNA library prepared from poly(A)+ RNA of ripe apple fruit. A 1.5-kb (kilobase) cDNA clone which hybridized to all three probes were isolated. The clone contained an open reading frame of 1214 base pairs (bp) encoding a sequence of 404 amino acids. While the polyadenine tail at the 3′-end was intact, it lacked a portion of sequence at the 5′-end. Using the RNA-based polymerase chain reaction, an additional sequence of 148 bp was obtained at the 5′-end. Thus, 1362 bp were sequenced and they encode 454 amino acids. The deduced amino-acid sequence contained peptide sequences corresponding to all ten tryptic fragments, confirming the identity of the cDNA clone. Comparison of the deduced amino-acid sequence between ACC synthase from apple fruit and those from tomato (Lycopersicon esculentum Mill.) and winter squash (Cucurbita maxima Duch.) fruits demonstrated the presence of seven highly conserved regions, including the previously identified region for the active site. The size of the translation product of ACC-synthase mRNA was similar to that of the mature protein on sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE), indicating that apple ACC-synthase undergoes only minor, if any, post-translational proteolytic processing. Analysis of ACC-synthase mRNA by in-vitro translation-immunoprecipitation, and by Northern blotting indicates that the ACC-synthase mRNA was undetectable in unripe fruit, but was accumulated massively during the ripening proccess. These data demonstrate that the expression of the ACC-synthase gene is developmentally regulated.
    Type of Medium: Electronic Resource
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