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Properties of the phosphorylation reaction catalyzed by SpoIIAB that help to regulate sporulation of Bacillus subtilis.由SpoIIAB催化的磷酸化反应的特性,有助于调节枯草芽孢杆菌的孢子形成。
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2
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Fate of the SpoIIAB*-ADP liberated after SpoIIAB phosphorylates SpoIIAA of Bacillus subtilis.枯草芽孢杆菌SpoIIAB使SpoIIAA磷酸化后释放的SpoIIAB*-ADP的去向。
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Establishing differential gene expression in sporulating Bacillus subtilis: phosphorylation of SpoIIAA (anti-anti-sigmaF) alters its conformation and prevents formation of a SpoIIAA/SpoIIAB/ADP complex.在枯草芽孢杆菌芽孢形成过程中建立差异基因表达:SpoIIAA(抗抗σF)的磷酸化改变其构象并阻止SpoIIAA/SpoIIAB/ADP复合物的形成。
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Fate of the SpoIIAB*-ADP liberated after SpoIIAB phosphorylates SpoIIAA of Bacillus subtilis.枯草芽孢杆菌SpoIIAB使SpoIIAA磷酸化后释放的SpoIIAB*-ADP的去向。
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7
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本文引用的文献

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Contribution of partner switching and SpoIIAA cycling to regulation of sigmaF activity in sporulating Bacillus subtilis.伴侣切换和SpoIIAA循环对枯草芽孢杆菌孢子形成过程中σF活性调控的贡献。
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Bifunctional protein required for asymmetric cell division and cell-specific transcription in Bacillus subtilis.枯草芽孢杆菌不对称细胞分裂和细胞特异性转录所需的双功能蛋白。
Genes Dev. 1996 Apr 1;10(7):794-803. doi: 10.1101/gad.10.7.794.
3
Structure and function of the Bacillus SpoIIE protein and its localization to sites of sporulation septum assembly.芽孢杆菌SpoIIE蛋白的结构与功能及其在芽孢形成隔膜组装位点的定位
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Establishing differential gene expression in sporulating Bacillus subtilis: phosphorylation of SpoIIAA (anti-anti-sigmaF) alters its conformation and prevents formation of a SpoIIAA/SpoIIAB/ADP complex.在枯草芽孢杆菌芽孢形成过程中建立差异基因表达:SpoIIAA(抗抗σF)的磷酸化改变其构象并阻止SpoIIAA/SpoIIAB/ADP复合物的形成。
Mol Microbiol. 1996 Feb;19(4):901-7. doi: 10.1046/j.1365-2958.1996.434964.x.
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SpoIIAA governs the release of the cell-type specific transcription factor sigma F from its anti-sigma factor SpoIIAB.SpoIIAA调控细胞类型特异性转录因子σF从其抗σ因子SpoIIAB中释放出来。
J Mol Biol. 1996 Jul 12;260(2):147-64. doi: 10.1006/jmbi.1996.0389.
6
SpoIIE governs the phosphorylation state of a protein regulating transcription factor sigma F during sporulation in Bacillus subtilis.SpoIIE调控枯草芽孢杆菌芽孢形成过程中一种调节转录因子sigma F的蛋白质的磷酸化状态。
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SpoIIAB is an anti-sigma factor that binds to and inhibits transcription by regulatory protein sigma F from Bacillus subtilis.SpoIIAB是一种抗σ因子,它能结合并抑制来自枯草芽孢杆菌的调控蛋白σF的转录作用。
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Sigma F, the first compartment-specific transcription factor of B. subtilis, is regulated by an anti-sigma factor that is also a protein kinase.Sigma F是枯草芽孢杆菌的首个特定区室转录因子,由一种同时也是蛋白激酶的抗Sigma因子调控。
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The importance of morphological events and intercellular interactions in the regulation of prespore-specific gene expression during sporulation in Bacillus subtilis.形态学事件和细胞间相互作用在枯草芽孢杆菌芽孢形成过程中对芽孢前体特异性基因表达调控中的重要性。
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10
An adenosine nucleotide switch controlling the activity of a cell type-specific transcription factor in B. subtilis.一种控制枯草芽孢杆菌中细胞类型特异性转录因子活性的腺苷核苷酸开关。
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由SpoIIAB催化的磷酸化反应的特性,有助于调节枯草芽孢杆菌的孢子形成。

Properties of the phosphorylation reaction catalyzed by SpoIIAB that help to regulate sporulation of Bacillus subtilis.

作者信息

Najafi S M, Harris D A, Yudkin M D

机构信息

Department of Biochemistry, University of Oxford, United Kingdom.

出版信息

J Bacteriol. 1997 Sep;179(17):5628-31. doi: 10.1128/jb.179.17.5628-5631.1997.

DOI:10.1128/jb.179.17.5628-5631.1997
PMID:9287028
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC179444/
Abstract

Phosphorylation of SpoIIAA on Ser-58 catalyzed by SpoIIAB is important in the regulation of sporulation of Bacillus subtilis. Nucleotide binding experiments showed that the affinity of SpoIIAB for ATP was greatly increased in the presence of SpoIIAA or a mutant SpoIIAA in which Ser-58 had been changed to alanine. Study of the phosphorylation reaction showed that the Km for ATP and the Ki for ADP were both about 1 microM. The kinetics of phosphorylation of SpoIIAA by SpoIIAB were biphasic, comprising a rapid phase (leading to phosphorylation of 1 mol of SpoIIAA/mol of SpoIIAB) followed by a slower, steady-state phase. In the steady state, the rate-determining step proved to be the dissociation of a SpoIIAB-ADP complex. The rate of this dissociation was not affected significantly by changes in the concentration of ATP.

摘要

由SpoIIAB催化的SpoIIAA第58位丝氨酸的磷酸化在枯草芽孢杆菌芽孢形成的调控中起重要作用。核苷酸结合实验表明,在SpoIIAA或第58位丝氨酸已被替换为丙氨酸的SpoIIAA突变体存在的情况下,SpoIIAB对ATP的亲和力大大增加。磷酸化反应研究表明,ATP的米氏常数(Km)和ADP的抑制常数(Ki)均约为1微摩尔。SpoIIAB对SpoIIAA的磷酸化动力学呈双相,包括一个快速阶段(导致每摩尔SpoIIAB使1摩尔SpoIIAA磷酸化),随后是一个较慢的稳态阶段。在稳态下,限速步骤证明是SpoIIAB-ADP复合物的解离。该解离速率不受ATP浓度变化的显著影响。