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Protein kinase associated with chromatin and changes in substrate‐specificity during germination of wheat seeds
Author(s) -
Sasaki Kimiko,
Sugita Mamoru
Publication year - 1982
Publication title -
physiologia plantarum
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.351
H-Index - 146
eISSN - 1399-3054
pISSN - 0031-9317
DOI - 10.1111/j.1399-3054.1982.tb00317.x
Subject(s) - chromatin , biology , histone , seedling , biochemistry , germination , adp ribosylation , protein kinase a , kinase , microbiology and biotechnology , nad+ kinase , enzyme , botany , dna
Protein kinase activity was associated with chromatin in wheat ( Triticum aestivum L. cv. Mukakomugi) embryos. The kinase activity did not change significantly during germination, whereas the activity of poly (ADP‐ribose) synthetase decreased significantly. The protein kinase activity in chromatin was inhibited by NAD, NADH, and ADP‐ribose, and was enhanced by treatment of the chromatin with snake venom phosphodiesterase or soybean trypsin inhibitor. The activity in chromatin was not stimulated by cyclic AMP. Different subfractions of the histones, H1 and H2, were mainly phosphorylated in germ and 3 day‐germinated seedling chromatins. The histones, H3 and H4, seemed unable to accept phosphate from ATP in the in vitro reaction system. Different acidic non‐histone chromosomal proteins were phosphorylated in germ and 3‐day‐germinated seedling chromations, and germ‐specific and seedling‐specific acidic non‐histone chromosomal proteins seemed unable to accept phosphate from ATP.