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Periplasmic quality control in biogenesis of outer membrane proteins
- Source :
- Biochemical Society Transactions. 43:133-138
- Publication Year :
- 2015
- Publisher :
- Portland Press Ltd., 2015.
-
Abstract
- The β-barrel outer membrane proteins (OMPs) are integral membrane proteins that reside in the outer membrane of Gram-negative bacteria and perform a diverse range of biological functions. Synthesized in the cytoplasm, OMPs must be transported across the inner membrane and through the periplasmic space before they are assembled in the outer membrane. In Escherichia coli, Skp, SurA and DegP are the most prominent factors identified to guide OMPs across the periplasm and to play the role of quality control. Although extensive genetic and biochemical analyses have revealed many basic functions of these periplasmic proteins, the mechanism of their collaboration in assisting the folding and insertion of OMPs is much less understood. Recently, biophysical approaches have shed light on the identification of the intricate network. In the present review, we summarize recent advances in the characterization of these key factors, with a special emphasis on the multifunctional protein DegP. In addition, we present our proposed model on the periplasmic quality control in biogenesis of OMPs.
- Subjects :
- Protein Folding
Biology
Biochemistry
Biophysical Phenomena
Escherichia coli
Inner membrane
Outer membrane efflux proteins
Integral membrane protein
Heat-Shock Proteins
Escherichia coli Proteins
Serine Endopeptidases
Periplasmic space
Peptidylprolyl Isomerase
Cell biology
DNA-Binding Proteins
Periplasm
Translocase of the inner membrane
bacteria
Protein folding
Periplasmic Proteins
Carrier Proteins
Bacterial outer membrane
Biogenesis
Bacterial Outer Membrane Proteins
Molecular Chaperones
Subjects
Details
- ISSN :
- 14708752 and 03005127
- Volume :
- 43
- Database :
- OpenAIRE
- Journal :
- Biochemical Society Transactions
- Accession number :
- edsair.doi.dedup.....0c2e9915ce45fbaa7d825dbaefa61eda
- Full Text :
- https://doi.org/10.1042/bst20140217