Cytochalasin A inhibits the binding of phenylalanine ammonia-lyase mRNA to ribosomes during induction of phytoalexin in pea seedlings.
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.
Sugimoto
M
M
Laboratory of Plant Pathology and Genetic Engineering, Faculty of Agriculture, Okayama University, Japan.
Toyoda
K
K
Ichinose
Y
Y
Yamada
T
T
Shiraishi
T
T
D001578:Benzopyrans / Q000378:metabolism; D003572:Cytochalasins; D018532:Pisum sativum / Q000378:metabolism*; D010650:Phenylalanine Ammonia-Lyase / Q000235:genetics* / Q000378:metabolism; D010936:Plant Extracts / Q000378:metabolism*; D036343:Pterocarpans; D012333:RNA, Messenger / Q000378:metabolism*; D012270:Ribosomes / Q000378:metabolism*; D012639:Seeds; D012717:Sesquiterpenes; D013729:Terpenes; D000094162:Phytoalexins
D001578:Benzopyrans; D003572:Cytochalasins; D010936:Plant Extracts; D036343:Pterocarpans; D012333:RNA, Messenger; D012717:Sesquiterpenes; D013729:Terpenes; C031218:cytochalasin A; D010650:Phenylalanine Ammonia-Lyase; C003161:pisatin; D000094162:Phytoalexins