枯草芽孢杆菌孢子形成特异性σF的抗抗σ因子SpoIIAA的磷酸化位点。
Site of phosphorylation of SpoIIAA, the anti-anti-sigma factor for sporulation-specific sigma F of Bacillus subtilis.
作者信息
Najafi S M, Willis A C, Yudkin M D
机构信息
Department of Biochemistry, University of Oxford, United Kingdom.
出版信息
J Bacteriol. 1995 May;177(10):2912-3. doi: 10.1128/jb.177.10.2912-2913.1995.
Abstract
Sigma F is regulated by an anti-sigma factor, SpoIIAB, and an anti-anti-sigma factor, SpoIIAA. SpoIIAB also functions as a phosphokinase which transfers phosphate from ATP to SpoIIAA; this phosphorylation is thought to be involved in the regulatory mechanism. By using [gamma-32P]ATP to phosphorylate SpoIIAA, cleaving the protein proteolytically, and analyzing the one resulting radiolabelled peptide by the Edman degradation procedure, we show that the site of phosphorylation in SpoIIAA is Ser-58.
摘要
Sigma F 由一个抗西格玛因子SpoIIAB和一个抗抗西格玛因子SpoIIAA调控。SpoIIAB还作为一种磷酸激酶，将磷酸基团从ATP转移到SpoIIAA；这种磷酸化作用被认为参与了调控机制。通过使用[γ-32P]ATP对SpoIIAA进行磷酸化，对该蛋白质进行蛋白酶解切割，并通过埃德曼降解程序分析产生的一个放射性标记肽段，我们发现SpoIIAA中的磷酸化位点是Ser-58。
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