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Protein phosphorylation in isolated nuclei from etiolated Avena seedlings Effects of red/far‐red light and cholera toxin
Author(s) -
Romero Luis C.,
Biswal Basanti,
Song Pill-Soon
Publication year - 1991
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 - 10.1016/0014-5793(91)80510-a
Subject(s) - cholera toxin , phosphorylation , dephosphorylation , etiolation , toxin , gtp' , biochemistry , protein phosphorylation , avena , western blot , biology , adp ribosylation , microbiology and biotechnology , protein kinase a , phosphatase , botany , enzyme , gene , nad+ kinase
We have studied the phosphorylation/dephosphorylation of several nuclear proteins in isolated nuclei from etiolated Avena seedlings as a function of red/far‐red light. The effect of stimulatory (ADP‐ribosylation by cholera toxin) or inhibitory (GDPβS) conditions for GTP‐binding proteins was also studied. Red or far‐red light enhanced the phosphorylation level of 2 nuclear proteins with molecular masses of 75 and 60 kDa. The phosphorylation pattern was affected by the addition of cholera toxin or GDPβS to the isolated nuclei. At least 2 proteins with molecular masses of 24 and 75 kDa cross‐reacted by Westerrs blot with GTP‐binding protein antibodies.