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A Heat‐Stress Pulse Inactivates a 50 kDa Myelin Basic Protein Kinase in Tomato
Author(s) -
Heider H.,
Boscheinen O.,
Scharf K.D.
Publication year - 1998
Publication title -
botanica acta
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.871
H-Index - 87
eISSN - 1438-8677
pISSN - 0932-8629
DOI - 10.1111/j.1438-8677.1998.tb00725.x
Subject(s) - cycloheximide , kinase , protein kinase a , myelin basic protein , mitogen activated protein kinase kinase , cyclin dependent kinase 9 , cyclin dependent kinase 2 , microbiology and biotechnology , in vitro , biochemistry , ask1 , chemistry , myelin , biology , protein biosynthesis , endocrinology , central nervous system
The involvement of kinases in heat stress signaling in tomato cells was studied by in gel kinase assays using myelin basic protein as substrate, and by in vitro phosphorylation assays in Mono Q fractions of tomato cell lysates. A kinase with an apparent molecular mass of approximately 50 kDa is rapidly deactivated upon heat stress as judged from in gel kinase assays. Cycloheximide treatment increases kinase activity, but concomitant heat treatment abolishes cycloheximide‐induced activation. Kinase activity from untreated cells was recovered at about 130 and 250 mM NaCl from Mono Q columns.