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Light signals are transduced to the phosphorylation of 15 kDa proteins in Neurospora crassa
Author(s) -
Oda Kazushi,
Hasunuma Kohji
Publication year - 1994
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(94)00436-6
Subject(s) - neurospora crassa , phosphorylation , neurospora , protein phosphorylation , microbiology and biotechnology , biochemistry , crassa , chemistry , biology , protein kinase a , gene , mutant
A microsomal fraction prepared from the mycelia of the band ( bd ) strain of Neurospora crassa showed enhanced phosphorylation of two small proteins with molecular masses of around 15 kDa (ps15) by the irradiation of the reaction mixture containing [γ‐ 32 P]ATP at 0°C for 1 s with blue light (450 nm, 6 μmol/m 2 /s or 420 nm, 80 μmol/m 2 /s). The reaction was stopped at 5 s of incubation at 0°C after blue light irradiation. The light effect could not be detected in ps15, when a microsomal fraction from a blind mutant, wc‐1 or wc‐2 was used. The mixing followed by homogenization of the microsomal fractions from wc‐1 and wc‐2 restored the activity to stimulate the phosphorylation of ps15 by blue light. The phosphorylated amino acid residue of ps15 was unstable when the proteins on a nylon membrane were exposed to an acid or alkaline solution, suggesting that the phosphorylated residue was aspartic acid. The other phosphorylated protein with a molecular mass of 70 kDa (p70) showed no light effect in the phosphorylation and the phosphorylated residue was estimated to be histidine, since it was stable in alkaline solution.