Microcystin affinity purification of plant protein phosphatases: PP1C, PP5 and a regulatory A-subunit of PP2A
Microcystin affinity purification of plant protein phosphatases: PP1C, PP5 and a regulatory A-subunit of PP2A
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DOI：
10.1016/s0014-5793(99)01093-5
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发表时间：
1999-09-03
期刊：
影响因子：
3.5
通讯作者：
MacKintosh, C
中科院分区：
文献类型：
--
作者：
Meek, S;Morrice, N;MacKintosh, C
通过微囊藻毒素-琼脂糖凝胶色谱法从花椰菜提取物中纯化了类似于35，55和65 kDa的蛋白质，并通过氨基酸序列测定分别鉴定为植物形式的蛋白（丝氨酸/苏氨酸）磷酸酶1（PP 1）催化亚基，PP 5和PP 2A的调节A亚基。鉴定了对应于三联肽（TPR）重复序列和PP 5催化结构域的肽。与哺乳动物PP 5类似，植物PP 5的酪蛋白磷酸酶活性被花生四烯酸激活> 10倍，在类似于100 μ M脂质时发生半数最大刺激（C）1999欧洲生物化学学会联合会。
Proteins of similar to 35, 55 and 65 kDa were purified from cauliflower extracts by microcystin-Sepharose chromatography and identified by amino acid sequencing as plant forms of protein (serine/threonine) phosphatase 1 (PP1) catalytic subunit, PP5 and a regulatory A-subunit of PP2A, respectively. Peptides that corresponded both to the tetratricopeptide (TPR) repeat and catalytic domains of PP5 were identified. Similar to mammalian PP5, the casein phosphatase activity of plant PP5 was activated > 10-fold by arachidonic acid, with half-maximal stimulation occurring at similar to 100 mu M lipid (C) 1999 Federation of European Biochemical Societies.