1997年3月
Effect of abscisic acid on phosphatidylserine-sensitive calcium dependent protein kinase activity and protein phosphorylation in rice
BIOSCIENCE BIOTECHNOLOGY AND BIOCHEMISTRY
- ,
- ,
- 巻
- 61
- 号
- 3
- 開始ページ
- 418
- 終了ページ
- 423
- 記述言語
- 英語
- 掲載種別
- DOI
- 10.1271/bbb.61.418
- 出版者・発行元
- TAYLOR & FRANCIS LTD
Protein kinase activity in the embryos of rice (Oryza sativa L. cv. Nipponbare) during seed soaking in water was assessed under various conditions, The histone III-S phosphorylating activity in the membrane fraction prepared from control seedlings treated with water was increased by the addition of Ca2+ (0.2 mM), and it increased further up on the simultaneous addition of phosphatidylserine (PS), By contrast, the activity in extracts prepared from ABA-treated seeds increased by Ca2+ alone and PS did not augment this increased level of activity, In vitro phosphorylation of the membrane fraction from control seeds in the presence of Ca2+ and PS resulted in phosphorylation of two proteins with molecular masses and isoelectric points of 40 kDa/8.9 and 40 kDa/7.6, respectively, When seeds were treated with exogenous ABA, phosphorylation in vitro of these two proteins was dependent only on the addition of Ca2+, N-(6-Aminohexyl)-5-chloro-1-naphthalenesulfonamide hydrochloride (W-7) did not block phosphorylation of these proteins, which is dependent on Ca2+, The varieties and quantities of phospholipids in the seeds after soaking in water containing ABA were the same as those after soaking only in water, Phosphorylation of the 40-kDa proteins in vitro in the membrane fraction from control seeds required higher Ca2+ concentrations (1-2 mM) compared to that observed in the membrane fraction from ABA-treated seeds.
- リンク情報
- ID情報
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- DOI : 10.1271/bbb.61.418
- ISSN : 0916-8451
- eISSN : 1347-6947
- CiNii Articles ID : 110002678495
- Web of Science ID : WOS:A1997WQ21600003