Stepwise disassembly and apparent nonstepwise reassembly for the oligomeric RbsD protein
| Autor: | Xinmiao Fu, Zengyi Chang, Yongjun Feng, Wangwang Jiao |
|---|---|
| Rok vydání: | 2006 |
| Předmět: |
Protein Folding
Circular dichroism Chaperonins Circular Dichroism Escherichia coli Proteins A protein medicine.disease_cause Biochemistry Article Chaperonin chemistry.chemical_compound Monomer Bacterial Proteins chemistry medicine Biophysics Urea Electrophoresis Gel Two-Dimensional Protein folding Dimerization Molecular Biology Polyacrylamide gel electrophoresis Escherichia coli Cellular proteins |
| Zdroj: | Protein Science. 15:1441-1448 |
| ISSN: | 1469-896X 0961-8368 |
| DOI: | 10.1110/ps.062175806 |
| Popis: | 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. |
| Databáze: | OpenAIRE |
| Externí odkaz: |
|
Plný text