Protein quality control in the bacterial periplasm
Open Access
- 7 May 2004
- journal article
- review article
- Published by Springer Nature in Microbial Cell Factories
- Vol. 3 (1) , 4
Abstract
The proper functioning of extracytoplasmic proteins requires their export to, and productive folding in, the correct cellular compartment. All proteins in Escherichia coli are initially synthesized in the cytoplasm, then follow a pathway that depends upon their ultimate cellular destination. Many proteins destined for the periplasm are synthesized as precursors carrying an N-terminal signal sequence that directs them to the general secretion machinery at the inner membrane. After translocation and signal sequence cleavage, the newly exported mature proteins are folded and assembled in the periplasm. Maintaining quality control over these processes depends on chaperones, folding catalysts, and proteases. This article summarizes the general principles which control protein folding in the bacterial periplasm by focusing on the periplasmic maltose-binding protein.Keywords
This publication has 102 references indexed in Scilit:
- X-ray structure of a protein-conducting channelNature, 2003
- The DsbA Signal Sequence Directs Efficient, Cotranslational Export of Passenger Proteins to the Escherichia coli Periplasm via the Signal Recognition Particle PathwayJournal of Bacteriology, 2003
- Signal Recognition Particle (SRP)-mediated Targeting and Sec-dependent Translocation of an Extracellular Escherichia coli ProteinJournal of Biological Chemistry, 2003
- Selective degradation of unfolded proteins by the self-compartmentalizing HtrA protease, a periplasmic heat shock protein in Escherichia coliJournal of Molecular Biology, 1999
- Proteolytic digestion of bacterial inclusion body proteins during dynamic transition between soluble and insoluble formsBiochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology, 1999
- Modular structure of the trigger factor required for high activity in protein foldingJournal of Molecular Biology, 1997
- Modulation of the Escherichia coliσE (RpoE) heat‐shock transcription‐factor activity by the RseA, RseB and RseC proteinsMolecular Microbiology, 1997
- Probing the Structural Role of an αβ Loop of Maltose-binding Protein by Mutagenesis: Heat-shock Induction by Loop Variants of the Maltose-binding Protein that Form Periplasmic Inclusion BodiesJournal of Molecular Biology, 1996
- The Cpx proteins of Escherichia coli K12Journal of Molecular Biology, 1988
- Silent and functional changes in the periplasmic maltose-binding protein of Escherichia coli K12Journal of Molecular Biology, 1987