Adler E, Donella-Deana A, Arigoni F, Pinna L A, Stragler P
Institut de Biologie Physico-Chimique, Paris, France.
Mol Microbiol. 1997 Jan;23(1):57-62. doi: 10.1046/j.1365-2958.1997.1801552.x.
Bacillus subtilis SpoIIE is a Ser protein phosphatase whose action on the phosphoprotein SpoIIAA triggers the cell type-specific activation of a sporulation transcription factor. Here we report that SpoIIE displays sequence similarity to the PP2C family of eukaryotic Ser/Thr protein phosphatases, and that residues common to these proteins are required for the function of both SpoIIE and TPD1, a yeast PP2C. These findings suggest that SpoIIE and the PP2C protein phosphatases are structurally related, and reveal a striking formal similarity between the SpoIIAA regulatory circuit and that of mammalian mitochondrial pyruvate dehydrogenase. This similarity may reflect an evolutionarily conserved mechanism of biological regulation based on the interplay of His protein kinase-like Ser kinases and PP2C-like protein phosphatases.
枯草芽孢杆菌SpoIIE是一种丝氨酸蛋白磷酸酶，其对磷酸化蛋白SpoIIAA的作用触发了芽孢形成转录因子的细胞类型特异性激活。在此我们报告，SpoIIE与真核丝氨酸/苏氨酸蛋白磷酸酶的PP2C家族显示出序列相似性，并且这些蛋白共有的残基对于SpoIIE和酵母PP2C TPD1的功能都是必需的。这些发现表明SpoIIE与PP2C蛋白磷酸酶在结构上相关，并揭示了SpoIIAA调节回路与哺乳动物线粒体丙酮酸脱氢酶调节回路之间惊人的形式相似性。这种相似性可能反映了基于组氨酸蛋白激酶样丝氨酸激酶和PP2C样蛋白磷酸酶相互作用的进化保守的生物调节机制。
