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Oligopeptide Competition Assay for Phosphorylation Site Determination
Published on: May 18, 2017
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化标志着蛋白质被Clp蛋白酶降解
Débora Broch Trentini1, Marcin Józef Suskiewicz1, Alexander Heuck1
1Research Institute of Molecular Pathology (IMP), Dr-Bohr-Gasse 7, 1030 Vienna, Austria.
Nature
|November 4, 2016
概括
研究人员发现氨酸标记细菌蛋白质由ClpC-ClpP蛋白酶复合体降解. 这种细菌系统类似于真核生物中的泛素蛋白酶系统.
科学领域:
- 细菌蛋白质降解
- 蛋白酶的功能
- 翻译后的修改
背景情况:
- 蛋白质的循环对于细胞健康和信号传递至关重要.
- 细胞蛋白质的降解依赖于无处不在的标记.
- 之前还不知道细菌Clp蛋白酶的一般标记系统.
研究的目的:
- 阐明Bacillus subtilis中ClpC-ClpP蛋白质复合物的向机制.
- 为了识别细菌Clp蛋白酶的降解标签.
主要方法:
- 使用ClpP捕获突变物的定量亲和蛋白质组学.
- 在体外溶解实验.
- 高分辨率的共同晶体结构的确定.
主要成果:
- 在氨酸残留物上酸化的蛋白质被选择性地向ClpC-ClpP.
- 通过McsB激酶化是基质降解的必要和充分条件.
- 在ClpC ATPase上合的位点在结构上得到了解决.
结论:
- 氨酸作为ClpC-ClpP蛋白酶的降解标记.
- 这种酸标记系统在阳性细菌中保存.
- 该系统在功能上类似于真核生物的泛素蛋白酶体系统.
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