title: Interaction between bacterial outer membrane proteins and periplasmic quality control factors: a kinetic partitioning mechanism.
abstract: 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.
authors.affiliation: Beijing National Laboratory for Molecular Sciences, State Key Laboratory for Structural Chemistry of Unstable and Stable Species, Department of Chemical Biology, College of Chemistry and Molecular Engineering, and Biodynamic Optical Imaging Center, Peking University, Beijing 100871, China.
authors.forename: Si
authors.initials: S
authors.lastname: Wu
authors.forename: Xi
authors.initials: X
authors.lastname: Ge
authors.forename: Zhixin
authors.initials: Z
authors.lastname: Lv
authors.forename: Zeyong
authors.initials: Z
authors.lastname: Zhi
authors.forename: Zengyi
authors.initials: Z
authors.lastname: Chang
authors.forename: Xin Sheng
authors.initials: XS
authors.lastname: Zhao
mesh_terms: D001425:Bacterial Outer Membrane Proteins / Q000737:chemistry / Q000378:metabolism*; D002352:Carrier Proteins / Q000737:chemistry / Q000378:metabolism*; D004268:DNA-Binding Proteins / Q000737:chemistry / Q000378:metabolism*; D029968:Escherichia coli Proteins / Q000737:chemistry / Q000378:metabolism*; D031541:Fluorescence Resonance Energy Transfer; D006360:Heat-Shock Proteins / Q000737:chemistry / Q000378:metabolism*; D007700:Kinetics; D018832:Molecular Chaperones / Q000737:chemistry / Q000378:metabolism*; D019696:Peptidylprolyl Isomerase / Q000737:chemistry / Q000378:metabolism*; D019897:Periplasm / Q000378:metabolism; D033903:Periplasmic Proteins / Q000737:chemistry / Q000378:metabolism*; D018272:Porins / Q000737:chemistry / Q000378:metabolism*; D021381:Protein Transport; D012697:Serine Endopeptidases / Q000737:chemistry / Q000378:metabolism*
chemical_list: D001425:Bacterial Outer Membrane Proteins; D002352:Carrier Proteins; D004268:DNA-Binding Proteins; D029968:Escherichia coli Proteins; D006360:Heat-Shock Proteins; D018832:Molecular Chaperones; C113724:OmpC protein; D033903:Periplasmic Proteins; D018272:Porins; C072721:Skp protein, E coli; C061682:DegP protease; D012697:Serine Endopeptidases; C490900:SurA protein, E coli; D019696:Peptidylprolyl Isomerase