Interaction between bacterial outer membrane proteins and periplasmic quality control factors: a kinetic partitioning mechanism
| Autor: | Zengyi Chang, Si Wu, Zhixin Lv, Xinsheng Zhao, Zeyong Zhi, Xi Ge |
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| Rok vydání: | 2011 |
| Předmět: |
Porins
Biology medicine.disease_cause complex mixtures Biochemistry medicine Fluorescence Resonance Energy Transfer Molecular Biology Escherichia coli Heat-Shock Proteins Peptidylprolyl isomerase Escherichia coli Proteins Serine Endopeptidases Cell Biology Periplasmic space Peptidylprolyl Isomerase Transport protein DNA-Binding Proteins Kinetics Protein Transport Förster resonance energy transfer Periplasm Biophysics bacteria Periplasmic Proteins Bacterial outer membrane Carrier Proteins Function (biology) Biogenesis Bacterial Outer Membrane Proteins Molecular Chaperones |
| Zdroj: | The Biochemical journal. 438(3) |
| ISSN: | 1470-8728 |
| Popis: | The OMPs (outer membrane proteins) of Gram-negative bacteria have to be translocated through the periplasmic space before reaching their final destination. The aqueous environment of the periplasmic space and high permeability of the outer membrane engender such a translocation process inevitably challenging. In Escherichia coli, although SurA, Skp and DegP have been identified to function in translocating OMPs across the periplasm, their precise roles and their relationship remain to be elucidated. In the present paper, by using fluorescence resonance energy transfer and single-molecule detection, we have studied the interaction between the OMP OmpC and these periplasmic quality control factors. The results of the present study reveal that the binding rate of OmpC to SurA or Skp is much faster than that to DegP, which may lead to sequential interaction between OMPs and different quality control factors. Such a kinetic partitioning mechanism for the chaperone–substrate interaction may be essential for the quality control of the biogenesis of OMPs |
| Databáze: | OpenAIRE |
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