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  • 1
    Electronic Resource
    Electronic Resource
    Springer
    Plant molecular biology 5 (1985), S. 269-279 
    ISSN: 1573-5028
    Keywords: α-amylase ; barley ; sodium butyrate ; gene ; gibberellic acid ; mRNA
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Summary Sodium butyrate exerts a pronounced inhibition on the gibberellic acid-induced synthesis and secretion of α-amylase by aleurone cells of barley seeds. This inhibition, which is reversible and non-competitive with cespect to gibberellic acid, is concentration dependent, with virtually total inhibition being accomplished between 4 and 5 mM sodium butyrate. The pattern of inhibition of α-amylase formation correlates well with a decrease in the accumulation of its messenger RNA. The addition of butyrate 12 h after the addition of gibberellic acid to half-seeds, has no effect on the formation and secretion of α-amylase. It has been shown in earlier studies that the synthesis of α-amylase mRNAs takes about 12 h for completion. The conclusion that butyrate interferes with some step in the transcriptional process is supported by a decrease observed in the RNAs that hybridize with a cloned α-amylase cDNA. The results of in vitro translation confirm the inhibition of the formation of several translatable mRNAs. Further, immunological probing detected only trace amounts of α-amylase proteins in the secretion of butyrate-treated seeds. Translation of functional mRNAs, post-translational modifications and the secretion α-amylase are not affected by sodium butyrate. It is concluded that butyrate selectively inhibits the transcription of several genes that are under the influence of gibberellic acid. This report is the first one documenting the inhibitory effect of sodium butyrate on a hormone-induced synthesis and accumulation of mRNAs in a plant system.
    Type of Medium: Electronic Resource
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  • 2
    Electronic Resource
    Electronic Resource
    Springer
    Plant molecular biology 2 (1983), S. 249-258 
    ISSN: 1573-5028
    Keywords: barley ; α-amylase mRNA ; gibberellic acid ; abscisic acid ; aminoethyl cysteine
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract The changes in the levels of α-amylase mRNA is barley aleurone layers in response to addition of plant growth regulators have been studied using a cloned α-amylase cDNA as the hybridization probe. An increase in gibberellic acid (GA) concentration in the incubation medium from 10−9 M to 10−6 M results in a progressive increase in α-amylase mRNA concentration in the aleurone cells. Detectable levels of α-amylase mRNA appear in the aleurone cells as early as 1 h after addition of GA. The concentration of this mRNA increases for several hours and then declines rapidly. Abscisic acid (ABA) and the amino acid analog S-2-aminoethyl-L-cysteine (AEC) suppress the GA-mediated induction of α-amylase. These compounds appear to affect the level of α-amylase mRNA in aleurone cells as measured byin vitro translation assays and by analysis of RNA blots with α-amylase cDNA probes. It is concluded that the regulation of α-amylase gene expression by ABA is at the level of transcription. Further, a protein factor appears to be required in addition to GA for transcription of α-amylase genes.
    Type of Medium: Electronic Resource
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  • 3
    ISSN: 1617-4623
    Keywords: Chloroplast ; RNA polymerase ; Deletion ; Cytoplasmic male sterility ; Sorghum
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Summary Fertile lines of sorghum (Sorghum bicolor) were shown to differ from cytoplasmic male sterile (CMS) lines by the presence of a 3.8 kb HindIII chloroplast DNA fragment in the former and a smaller (3.7 kb) fragment in the latter. DNA/DNA hybridization studies showed that these two fragments are homologous. Fertile plants from S. versicolor, S. almum, S. halepense, and Sorghastrum nutans (Yellow Indiangrass) also have the 3.8 kb fragment, and CMS lines studied containing A1, A2 and A3 cytoplasms have the 3.7 kb fragment. The size difference between the two fragments was localized to a 1.0 kb SacI-HindIII fragment by restriction mapping. A r65 by deletion, which is flanked by a 51 by tandem repeat, was identified in the CMS lines by sequencing the clones. Comparison of the two sequences with those from maize, rice, tobacco, spinach, pea, and liverwort revealed that the deleted sequence is located in the middle of the RNA polymerase β″ subunit encoded by the gene rpoC2. The amino acid sequence deleted in the CMS lines is in a monocot-specific region which contains two protein motifs that are characteristic of several transcriptional activation factors, namely, a leucine zipper motif and an acidic domain capable of forming an amphipathic α-helix. Further studies designed to determine whether or not the deletion is involved in CMS of sorghum are underway.
    Type of Medium: Electronic Resource
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