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Protein Science (2006), 15:1441-1448. Published by Cold Spring Harbor Laboratory Press. Copyright © 2006 The Protein Society
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Stepwise disassembly and apparent nonstepwise reassembly for the oligomeric RbsD protein

Yongjun Feng1,4, Wangwang Jiao3, Xinmiao Fu3 and Zengyi Chang1,2,3

1 National Laboratory of Protein Engineering and Plant Genetics
2 College of Life Sciences
3 The Center for Protein Science, Peking University, Beijing 100871, P.R. China
4 School of Life Science and Technology, Beijing Institute of Technology, Beijing 100081, P.R. China

(RECEIVED February 21, 2006; FINAL REVISION March 20, 2006; ACCEPTED March 20, 2006)

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.

Keywords: RbsD; oligomeric protein; disassembly; reassembly; oligomeric intermediate


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