Cytochalasin A Inhibits the Binding of Phenylalanine Ammonia-Lyase mRNA to Ribosomes during induction of Phytoalexin in Pea Seedlings
Author(s) -
Manabu Sugimoto,
Kyohei Toyoda,
Yuki Ichinose,
Tetsuji Yokoyama,
Takuya Shiraishi
Publication year - 2000
Publication title -
plant and cell physiology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.975
H-Index - 152
eISSN - 1471-9053
pISSN - 0032-0781
DOI - 10.1093/pcp/41.2.234
Subject(s) - phenylalanine ammonia lyase , phytoalexin , elicitor , biochemistry , cytochalasin , phenylalanine , ribosome , messenger rna , biosynthesis , protein biosynthesis , cytochalasin b , chemistry , biology , enzyme , gene , cell , cytoskeleton , rna , amino acid , resveratrol
Cytochalasin A (CA) blocked the accumulation of phytoalexin and phenylalanine ammonia-lyase (PAL)-protein in pea tissues treated with a fungal elicitor but scarcely affected the PAL-mRNA content. Further analysis showed that CA decreased the PAL-mRNA bound to ribosomes. These results indicate that actin filaments are tightly associated with the translational process of the PAL gene.
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