Characterization of an unusual cold shock protein from Staphylococcus aureus.
Characterization of an unusual cold shock protein from Staphylococcus aureus.
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DOI：
10.1002/jobm.200900264
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发表时间：
2010-12
影响因子：
3.1
通讯作者：
Sau S
中科院分区：
文献类型：
--
作者：
Chanda PK;Bandhu A;Jana B;Mondal R;Ganguly T;Sau K;Lee CY;Chakrabarti G;Sau S
在由金黄色葡萄球菌表达的三种冷休克蛋白中，CspC受冷诱导较差，但受各种抗生素和有毒化学物质强烈诱导。使用纯化的CspC，在这里，我们证明它在溶液中作为单体存在，主要具有β-折叠，并与其他细菌Csps具有实质性的结构相似性。CspC的聚集在高于40 °C的温度下迅速开始，而在0 M GdmCl下CspC稳定化的吉布斯自由能估计为+1.6 kcal mol-1，表明蛋白质较不稳定。令人惊讶的是，CspC显示出与携带一段多于三个胸腺嘧啶碱基的ssDNA的稳定结合，并且与这样的ssDNA的结合不仅使CspC针对蛋白水解降解稳定，而且还淬灭了来自其暴露的Trp残基的荧光强度。淬灭数据的分析表明，每个CspC分子与上述ssDNA的~5个连续胸腺嘧啶碱基结合，并且结合本质上是协同的。
Of the three cold shock proteins expressed by Staphylococcus aureus, CspC is induced poorly by cold but strongly by various antibiotics and toxic chemicals. Using a purified CspC, here we demonstrate that it exists as a monomer in solution, possesses primarily β-sheets, and bears substantial structural similarity with other bacterial Csps. Aggregation of CspC was initiated rapidly at temperatures above 40 °C, whereas, the Gibbs free energy of stabilization of CspC at 0 M GdmCl was estimated to be +1.6 kcal mol–1, indicating a less stable protein. Surprisingly, CspC showed stable binding with ssDNA carrying a stretch of more than three thymine bases and binding with such ssDNA had not only stabilized CspC against proteolytic degradation but also quenched the fluorescence intensity from its exposed Trp residue. Analysis of quenching data indicates that each CspC molecule binds with ~5 contiguous thymine bases of the above ssDNA and binding is cooperative in nature.
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影响因子：
3.1
作者：
Chanda, Palas Kumar;Mondal, Rajkrishna;Sau, Subrata
通讯作者：
Sau, Subrata
影响因子：
4.8
作者：
Ganguly, Tridib;Bandhu, Amitava;Sau, Subrata
通讯作者：
Sau, Subrata
影响因子：
4.8
作者：
Lopez, MM;Yutani, K;Makhatadze, GI
通讯作者：
Makhatadze, GI
影响因子：
3.8
作者：
Das, Malabika;Ganguly, Tridib;Sau, Subrata
通讯作者：
Sau, Subrata
影响因子：
1.6
作者：
Garchow, BG;Jog, SP;Murthy, PPN
通讯作者：
Murthy, PPN