Opposing pairs of serine protein kinases and phosphatases transmit signals of environmental stress to activate a bacterial transcription factor.

Opposing pairs of serine protein kinases and phosphatases transmit signals of environmental stress to activate a bacterial transcription factor.
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DOI:
10.1101/gad.10.18.2265
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发表时间:
1996-09
影响因子:
10.5
通讯作者:
Xiaofeng Yang;Choong-Min Kang;M. S. Brody;C. Price
Xiaofeng Yang;Choong-Min Kang;M. S. Brody;C. Price
中科院分区:
生物学1区
文献类型:
--
作者:
Xiaofeng Yang;Choong-Min Kang;M. S. Brody;C. Price

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枯草芽孢杆菌的一般应激反应是由信号转导网络控制的,该网络调节sigma(B)转录因子的活性。我们发现该网络包括两个伙伴交换模块,RsbX-RsbS-RsbT和RsbU-RsbV-RsbW,它们有助于调节sigma(B)。每个模块由一个磷酸酶(X或U)、一个拮抗剂蛋白(S或V)和一个开关蛋白/激酶(T或W)组成。在下游模块中,W抗sigma因子是sigma(B)活性的主要调节因子。如果V拮抗剂被磷酸化,W开关蛋白结合并抑制sigma(B)。如果V未磷酸化,它与W复合物,释放sigma(B)与RNA聚合酶相互作用并促进转录。V的磷酸化状态受激酶(W)和磷酸酶(U)活性的抑制。U型磷酸酶由上游模块调控。T开关蛋白直接结合U,刺激磷酸酶活性。T- u相互作用由S拮抗剂的磷酸化状态控制,由相反的激酶(T)和磷酸酶(X)活性控制。这种伙伴转换机制提供了一种通用的调节策略,其中链接模块通过蛋白质-蛋白质相互作用感知和整合多种信号。
The general stress response of the bacterium Bacillus subtilis is governed by a signal transduction network that regulates activity of the sigma(B) transcription factor. We show that this network comprises two partner-switching modules, RsbX-RsbS-RsbT and RsbU-RsbV-RsbW, which contribute to regulating sigma(B). Each module consists of a phosphatase (X or U), an antagonist protein (S or V), and a switch protein/kinase (T or W). In the downstream module, the W anti-sigma factor is the primary regulator of sigma(B) activity. If the V antagonist is phosphorylated, the W switch protein binds and inhibits sigma(B). If V is unphosphorylated, it complexes W, freeing sigma(B) to interact with RNA polymerase and promote transcription. The phosphorylation state of V is controlled by opposing kinase (W) and phosphatase (U) activities. The U phosphatase is regulated by the upstream module. The T switch protein directly binds U, stimulating phosphatase activity. The T-U interaction is governed by the phosphorylation state of the S antagonist, controlled by opposing kinase (T) and phosphatase (X) activities. This partner-switching mechanism provides a general regulatory strategy in which linked modules sense and integrate multiple signals by protein-protein interaction.