Soll J, Buchanan B B
J Biol Chem. 1983 Jun 10;258(11):6686-9.
A new protein kinase of the cAMP independent type was found to be bound to the outer envelope membrane of spinach chloroplasts. While stimulated by Mg2+ and inhibited by ADP, the enzyme showed no response to conventional protein substrates and was essentially independent of pH in the physiological (pH 7 to 8) range. The new protein kinase phosphorylated the mature form of the small subunit of ribulose 1,5-bisphosphate carboxylase/oxygenase and, to a lesser extent, an unidentified 24-kDa polypeptide, both of which were bound to the outer envelope membrane. The results suggest that phosphorylation of cytoplasmically synthesized protein constituents of chloroplasts is involved in their transport through the chloroplast envelope membrane barrier.
发现一种新的非cAMP依赖性蛋白激酶与菠菜叶绿体的外被膜结合。该酶受Mg2+刺激，被ADP抑制，对传统蛋白质底物无反应，在生理（pH 7至8）范围内基本不受pH影响。这种新的蛋白激酶使核酮糖1,5 - 二磷酸羧化酶/加氧酶小亚基的成熟形式磷酸化，在较小程度上也使一种未鉴定的24 kDa多肽磷酸化，这两种物质都与外被膜结合。结果表明，叶绿体细胞质中合成的蛋白质成分的磷酸化参与了它们通过叶绿体包膜膜屏障的转运过程。
