寡聚体RbsD蛋白的逐步拆解和明显的非逐步重新组装。
Stepwise disassembly and apparent nonstepwise reassembly for the oligomeric RbsD protein.
作者信息
Feng Yongjun, Jiao Wangwang, Fu Xinmiao, Chang Zengyi
机构信息
National Laboratory of Protein Engineering and Plant Genetics, Peking University, Beijing 100871, PR China.
出版信息
Protein Sci. 2006 Jun;15(6):1441-8. doi: 10.1110/ps.062175806.
Many cellular proteins exist as homo-oligomers. The mechanism of the assembly process of such proteins is still poorly understood. We have previously observed that Hsp16.3, a protein exhibiting chaperone-like activity, undergoes stepwise disassembly and nonstepwise reassembly. Here, the disassembly and reassembly of a nonchaperone protein RbsD, from Escherichia coli, was studied in vitro. The protein was found to mainly exist as decamers with a small portion of apparently larger oligomeric forms, both of which are able to refold/reassemble effectively in a spontaneous way after being completely unfolded. Disassembly RbsD intermediates including pentamers, tetramers, trimers, dimers, and monomers were detected by using urea-containing pore gradient polyacrylamide gel electrophoresis, while only pentamers were detected for its reassembly. The observation of stepwise disassembly and apparent nonstepwise reassembly for both a chaperone protein (Hsp16.3) and a nonchaperone protein (RbsD) strongly suggests that such a feature is most likely general for homo-oligomeric proteins.
许多细胞蛋白质以同型寡聚体的形式存在。这类蛋白质组装过程的机制仍知之甚少。我们之前观察到，具有伴侣样活性的蛋白质Hsp16.3会经历逐步解聚和非逐步重新组装。在此，我们对来自大肠杆菌的非伴侣蛋白RbsD的解聚和重新组装进行了体外研究。该蛋白质主要以十聚体形式存在，还有一小部分明显更大的寡聚体形式，这两种形式在完全展开后都能够自发有效地重新折叠/重新组装。通过使用含尿素的孔梯度聚丙烯酰胺凝胶电泳检测到RbsD解聚中间体包括五聚体、四聚体、三聚体、二聚体和单体，而其重新组装过程中仅检测到五聚体。伴侣蛋白（Hsp16.3）和非伴侣蛋白（RbsD）都出现逐步解聚和明显的非逐步重新组装现象，这强烈表明这种特征很可能是同型寡聚体蛋白的普遍特征。
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