DEACTIVATION OF THE SPORULATION TRANSCRIPTION FACTOR SPO0A BY THE SPO0E PROTEIN PHOSPHATASE
DEACTIVATION OF THE SPORULATION TRANSCRIPTION FACTOR SPO0A BY THE SPO0E PROTEIN PHOSPHATASE
复制标题
DOI：
10.1073/pnas.91.5.1756
复制
发表时间：
1994-03-01
影响因子：
11.1
通讯作者：
HOCH, JA
中科院分区：
文献类型：
--
作者：
OHLSEN, KL;GRIMSLEY, JK;HOCH, JA
枯草芽孢杆菌的spoe基因座编码一种负调节产孢的基因，当这种基因过量产生时，会抑制产孢，如果被删除，则会导致产孢时间不适当。该位点的产物，spoe，被纯化并发现是一种蛋白磷酸酶，它特异性地去磷酸化类似于P的孢子转录因子spoa，将其转化为无活性形式。在磷酸化信号转导通路的其他组分上，spoe作为一种磷酸酶没有明显的活性，产生类似于P.的spoe蛋白突变体，导致产孢缺乏，被纯化后发现其作为一种磷酸酶异常活跃。spoe磷酸酶可以为环境、代谢或细胞周期对磷传递的调节提供额外的控制点。这些结果强化了这样一个概念，即磷中继受一系列孢子形成的正、负信号的影响，这些信号被识别并解释为一个信号集成电路，具有调节活性磷酸化的spoa孢子形成转录因子的细胞水平的作用。
The spoOE locus of Bacillus subtilis codes for a negative regulator of sporulation that, when overproduced, represses sporulation and, if deleted, results in inappropriate timing of sporulation. The product of this locus, SpoOE, was purified and found to be a protein phosphatase, which specifically dephosphorylated the sporulation transcription factor SpoOA similar to P, converting it to an inactive form. SpoOE was not significantly active as a phosphatase on other components of the phosphorelay signal-transduction pathway producing SpoOA similar to P. A mutant SpoOE protein that results in sporulation deficiency was purified and found to be hyperactive as a phosphatase. The SpoOE phosphatase may provide an additional control point for environmental, metabolic, or cell-cycle regulation of phosphate flow in the phosphorelay. These results reinforce the concept that the phosphorelay is subject to a host of positive and negative signals for sporulation that are recognized and interpreted as a signal integration circuit that has the role of regulating the cellular level of active phosphorylated SpoOA sporulation transcription factor.