叶绿体ATP合酶（CF0CF1 - ATP酶）的β亚基被酪蛋白激酶II磷酸化。
The beta subunit of chloroplast ATP synthase (CF0CF1-ATPase) is phosphorylated by casein kinase II.
作者信息
Kanekatsu M, Saito H, Motohashi K, Hisabori T
机构信息
Laboratory of Biology, Kitasato University, Sagamihara, Japan.
出版信息
Biochem Mol Biol Int. 1998 Sep;46(1):99-105. doi: 10.1080/15216549800203602.
We studied a phosphate acceptor for casein kinase II (CK-II) in chloroplasts, and found a 56 kDa protein (p56) as an acceptor, which was partially purified from the stroma of spinach chloroplasts. The N-terminal amino acid sequence of p56 was identical with that of the beta subunit of chloroplast ATP synthase (CF0CF1-ATPase). In addition, the recombinant beta subunit of CF1 was phosphorylated when the subunit was incubated with CK-II. These results suggest that the beta subunit of CF1 is a substrate protein of CK-II in the chloroplast.
我们研究了叶绿体中酪蛋白激酶II（CK-II）的磷酸受体，发现一种56 kDa的蛋白质（p56）作为受体，它是从菠菜叶绿体基质中部分纯化得到的。p56的N端氨基酸序列与叶绿体ATP合酶（CF0CF1-ATPase）的β亚基相同。此外，当CF1的重组β亚基与CK-II一起温育时，该亚基会被磷酸化。这些结果表明，CF1的β亚基是叶绿体中CK-II的底物蛋白。
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