Stepwise disassembly and apparent nonstepwise reassembly for the oligomeric RbsD protein
Stepwise disassembly and apparent nonstepwise reassembly for the oligomeric RbsD protein
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DOI：
10.1110/ps.062175806
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发表时间：
2006-06
期刊：
影响因子：
8
通讯作者：
Yongjun Feng;Wangwang Jiao;Xinmiao Fu;Z. Chang
中科院分区：
文献类型：
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作者：
Yongjun Feng;Wangwang Jiao;Xinmiao Fu;Z. Chang
许多细胞蛋白质以同源寡聚体形式存在。此类蛋白质组装过程的机制仍然知之甚少。我们以前观察到，Hsp16.3，一种表现出分子伴侣样活性的蛋白质，经历逐步拆卸和非逐步重组。在这里，拆卸和重组的非伴侣蛋白RbsD，从大肠杆菌，在体外进行了研究。发现该蛋白质主要以十聚体形式存在，具有一小部分明显较大的寡聚体形式，两者都能够在完全展开后以自发方式有效地重新折叠/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的拆解中间体，包括五聚体、四聚体、三聚体、二聚体和单体，而仅检测到五聚体用于其重新组装。分子伴侣蛋白（Hsp16.3）和非分子伴侣蛋白（RbsD）的逐步分解和明显的非逐步重组的观察强烈表明，这种特征很可能是同源寡聚蛋白质的普遍特征。
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.