The jasmonate-induced 60 kDa protein of barley exhibits N-glycosidase activity in vivo.
Upon jasmonate treatment barley leaf segments express a putative ribosome-inactivating protein (JIP60). The influence of this protein on translation in planta has been analysed by using barley plants and tobacco plants transformed with a barley cDNA encoding JIP60. In both plant systems JIP60 exhibited N-glycosidase activity in vivo. The depurination of the 25S rRNA of tobacco and barley ribosomes led to accumulation of translationally inactive polysomes.
Dunaeva
M
M
Institut fur Pflanzenbiochemie, Halle/Saale, Germany. marina@biokemi.su.se
Goebel
C
C
Wasternack
C
C
Parthier
B
B
Goerschen
E
E
D002474:Cell-Free System; D003517:Cyclopentanes / Q000494:pharmacology*; D004790:Enzyme Induction; D006026:Glycoside Hydrolases / Q000235:genetics* / Q000302:isolation & purification / Q000378:metabolism; D001467:Hordeum / Q000187:drug effects* / Q000378:metabolism; D007700:Kinetics; D008970:Molecular Weight; D054883:Oxylipins; D010937:Plant Growth Regulators / Q000494:pharmacology; D018515:Plant Leaves; D010940:Plant Proteins / Q000235:genetics* / Q000302:isolation & purification / Q000378:metabolism; D010947:Plants, Toxic; D014176:Protein Biosynthesis; D012270:Ribosomes / Q000378:metabolism* / Q000648:ultrastructure; D014026:Nicotiana / Q000378:metabolism
D003517:Cyclopentanes; C091875:JIP60 protein, Hordeum vulgare; D054883:Oxylipins; D010937:Plant Growth Regulators; D010940:Plant Proteins; C011006:jasmonic acid; D006026:Glycoside Hydrolases