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Stepwise disassembly and apparent nonstepwise reassembly for the oligomeric RbsD protein
Author(s) -
Feng Yongjun,
Jiao Wangwang,
Fu Xinmiao,
Chang Zengyi
Publication year - 2006
Publication title -
protein science
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 3.353
H-Index - 175
eISSN - 1469-896X
pISSN - 0961-8368
DOI - 10.1110/ps.062175806
Subject(s) - chaperone (clinical) , monomer , chemistry , protein folding , biochemistry , oligomer , protein aggregation , polyacrylamide gel electrophoresis , biophysics , biology , enzyme , polymer , medicine , organic chemistry , pathology
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.