Stepwise disassembly and apparent nonstepwise reassembly for the oligomeric RbsD protein.
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.
Feng
Yongjun
Y
National Laboratory of Protein Engineering and Plant Genetics, Peking University, Beijing 100871, PR China.
Jiao
Wangwang
W
Fu
Xinmiao
X
Chang
Zengyi
Z
D001426:Bacterial Proteins / Q000737:chemistry / Q000378:metabolism; D018833:Chaperonins / Q000737:chemistry / Q000378:metabolism; D002942:Circular Dichroism; D019281:Dimerization; D015180:Electrophoresis, Gel, Two-Dimensional / Q000379:methods; D029968:Escherichia coli Proteins / Q000737:chemistry* / Q000378:metabolism*; D017510:Protein Folding; D014508:Urea / Q000737:chemistry
D001426:Bacterial Proteins; D029968:Escherichia coli Proteins; C431133:Hsp16.3 protein, Mycobacterium tuberculosis; C512270:RbsD protein, E coli; D014508:Urea; D018833:Chaperonins