Induction of Expression of Genes Coding for Sporamin and β-Amylase by Polygalacturonic Acid in Leaf-Petiole Cuttings of Sweet Potato
Author(s) -
Masaaki Ohto,
K Nakamura-Kito,
K. Nakamura
Publication year - 1992
Publication title -
plant physiology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 3.554
H-Index - 312
eISSN - 1532-2548
pISSN - 0032-0889
DOI - 10.1104/pp.99.2.422
Subject(s) - abscisic acid , biochemistry , sucrose , petiole (insect anatomy) , methyl jasmonate , thaumatin , amylase , gene expression , starch , chemistry , biology , gene , botany , enzyme , hymenoptera
Sporamin and beta-amylase are two major proteins of tuberous storage root of sweet potato (Ipomoea batatas) and their accumulation can be induced concomitantly with the accumulation of starch in leaves and petioles by sucrose (K Nakamura, M Ohto, N Yoshida, K Nakamura [1991] Plant Physiol 96: 902-909). Although mechanical wounding of leaves of sweet potato only occasionally induced the expression of sporamin and beta-amylase genes, their expression could be reproducibly induced in leaf-petiole cuttings when these explants were dipped in a solution of polygalacturonic acid or chitosan at their cut edges. Polygalacturonic acid seemed to induce expression of the same genes coding for sporamin and beta-amylase that are induced by sucrose. Because polygalacturonic acid and chitosan are known to mediate the induction of wound-inducible defense reactions, these results raise an interesting possibility that beta-amylase, in addition to sporamin, may have some role in the defense reaction. Expression of sporamin and beta-amylase genes could also be induced by abscisic acid, and this induction by abscisic acid, as well as induction by polygalacturonic acid or sucrose, was repressed by gibberellic acid. By contrast, methyl jasmonate did not cause the significant induction of either sporamin or beta-amylase mRNAs. Induction of expression of sporamin and beta-amylase genes by polygalacturonic acid or sucrose was inhibited by cycloheximide, suggesting that de novo synthesis of proteins is required for both of the induction processes.
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