New insight into secreted ribonuclease structure: binase is a natural dimer.

New insight into secreted ribonuclease structure: binase is a natural dimer.
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DOI:
10.1371/journal.pone.0115818
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发表时间:
2014
期刊:
影响因子:
3.7
通讯作者:
Ilinskaya O
Ilinskaya O
中科院分区:
综合性期刊3区
文献类型:
--
作者:
Dudkina E;Kayumov A;Ulyanova V;Ilinskaya O

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核糖核酸酶(RNases)的生物学作用,如控制血管生长、对肿瘤细胞的毒性和抗病毒活性,需要详细解释。核糖核酸酶最有趣的特性之一是能够形成二聚体,这有助于有效的RNA水解和逃避核糖核酸酶抑制剂。由矮芽孢杆菌(原中间芽孢杆菌)分泌的二聚体形式的微生物RNase二酶迄今只在晶体中发现。我们的研究是第一个直接证实二酶二聚体存在于溶液中以及在酵素合成和分泌的自然条件下的报告。通过凝胶电泳、免疫印迹、尺寸排除色谱和质谱分析,我们发现binase是一种稳定的天然二聚体,具有高催化活性。
The biological effects of ribonucleases (RNases), such as the control of the blood vessels growth, the toxicity towards tumour cells and antiviral activity, require a detailed explanation. One of the most intriguing properties of RNases which can contribute to their biological effects is the ability to form dimers, which facilitates efficient RNA hydrolysis and the evasion of ribonuclease inhibitor. Dimeric forms of microbial RNase binase secreted by Bacillus pumilus (former B. intermedius) have only been found in crystals to date. Our study is the first report directly confirming the existence of binase dimers in solution and under natural conditions of enzyme biosynthesis and secretion by bacilli. Using different variants of gel electrophoresis, immunoblotting, size-exclusion chromatography and mass-spectrometry, we revealed that binase is a stable natural dimer with high catalytic activity.
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影响因子: 5.7
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