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The jasmonate‐induced 60 kDa protein of barley exhibits N ‐glycosidase activity in vivo
Author(s) -
Dunaeva Marina,
Goebel Cornelia,
Wasternack Claus,
Parthier Benno,
Goerschen Eckart
Publication year - 1999
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(99)00645-6
Subject(s) - polysome , ribosome , in vivo , hordeum vulgare , depurination , biochemistry , complementary dna , protein biosynthesis , jasmonate , messenger rna , ribosome inactivating protein , biology , translation (biology) , methyl jasmonate , chemistry , botany , gene , arabidopsis , rna , poaceae , genetics , dna , mutant
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.