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  • 1
    ISSN: 1432-2048
    Keywords: Key words:Allium (root development) ; Ascorbate ; Cell division ; Cell expansion ; Hydroxyproline-containing protein ; Root development
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract. Post-translational hydroxylation of peptide-bound proline residues, catalyzed by peptidyl-prolyl-4 hydroxylase (EC 1.14.11.2) using ascorbate as co-substrate, is a key event in the maturation of a number of cell wall-associated hydroxyproline-rich glycoproteins (HRGPs), including extensins and arabinogalactan-proteins, which are involved in the processes of wall stiffening, signalling and cell proliferation. Allium cepa L. roots treated with 3,4-DL-dehydroproline (DP), a specific inhibitor of peptidyl-prolyl hydroxylase, showed a 56% decrease in the hydroxyproline content of HRGP. Administration of DP strongly affected the organization of specialized zones of root development, with a marked reduction of the post-mitotic isodiametric growth zone, early extension of cells leaving the meristematic zone and a huge increase in cell size. Electron-microscopy analysis showed dramatic alterations both to the organization of newly formed cell walls and to the adhesion of the plasma membranes to the cell walls. Moreover, DP administration inhibited cell cycle progression. Root tips grown in the presence of DP also showed an increase both in ascorbate content (+53%) and ascorbate-specific peroxidase activity in the cytosol (+72%), and a decrease in extracellular “secretory” peroxidase activity (−73%). The possible interaction between HRGPs and the ascorbate system in the regulation of both cell division and extension is discussed.
    Type of Medium: Electronic Resource
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  • 2
    ISSN: 1573-5028
    Keywords: Capsicum annuum ; endo-β-(1,4)-glucanase ; ethylene ; leaf abscission ; nucleotide sequence ; ripening
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract Ethylene promotes the abscission of leaves and the ripening of fruits in pepper plants, and in both events an increase in cellulase activity is observed. However, two enzyme isoforms (pI 7.2 and 8.5, respectively) are differentially involved in the two physiological phenomena. The pI 8.5 form has been purified from ripe fruits. It is a glycoprotein with an apparent molecular mass of 54 kDa. Two short peptides were sequenced and a very high homology to a tomato cellulase was observed. Polyclonal antibodies, raised against the purified enzyme, have allowed us to demonstrate that the observed ethylene-induced increase in cellulase activity is paralleled by de novo synthesis of protein. Three cDNAs (CX1, CX2 and CX3), encoding different cellulases, were obtained and characterized and their expression investigated. Accumulation of all three mRNAs is induced by ethylene treatment, though to different levels. CX1 is mainly expressed in ripe fruits while CX2 is especially found in abscission zones. CX3 accumulates at very low levels in activated abscission zones. Comparisons with other known cellulases demonstrate clear heterogeneity within the higher plant cellulases. Differences in ethylene inducibility and molecular structure suggest different physiological roles for cellulase in pepper plants.
    Type of Medium: Electronic Resource
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  • 3
    ISSN: 1615-6102
    Keywords: Spinacia oleracea L. ; Chloroplast ontogenesis ; Chloroplast senescence ; Spinach chloroplasts ; Intrathylakoidal crystals
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Summary The entire vital cycle of chloroplasts was followed in spinach leaves, in order to determine the plastidial situations leading to the build-up of intrathylakoidal crystals. This kind of inclusion was noticed in the juvenile ontogenetic stages as well as in the senescent chloroplast stage, while intrathylakoidal crystals were not present in the mature organelles. The appearance of such crystals, which are known to consist of ribulose 1,5-diphosphate carboxylase, is interpreted as a consequence of an imbalance between enzyme level and membrane function.
    Type of Medium: Electronic Resource
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