Biology of type II secretion
Top Cited Papers
- 1 April 2001
- journal article
- review article
- Published by Wiley in Molecular Microbiology
- Vol. 40 (2) , 271-283
- https://doi.org/10.1046/j.1365-2958.2001.02403.x
Abstract
The type II secretion pathway or the main terminal branch of the general secretion pathway, as it has also been referred to, is widely distributed among Proteobacteria, in which it is responsible for the extracellular secretion of toxins and hydrolytic enzymes, many of which contribute to pathogenesis in both plants and animals. Secretion through this pathway differs from most other membrane transport systems, in that its substrates consist of folded proteins. The type II secretion apparatus is composed of at least 12 different gene products that are thought to form a multiprotein complex, which spans the periplasmic compartment and is specifically required for translocation of the secreted proteins across the outer membrane. This pathway shares many features with the type IV pilus biogenesis system, including the ability to assemble a pilus‐like structure. This review discusses recent findings on the organization of the secretion apparatus and the role of its various components in secretion. Different models for pilus‐mediated secretion through the gated pore in the outer membrane are also presented, as are the possible properties that determine whether a protein is recognized and secreted by the type II pathway.Keywords
This publication has 93 references indexed in Scilit:
- Alteration of a single tryptophan residue of the cellulose-binding domain blocks secretion of the Erwinia chrysanthemiCel5 cellulase (ex-EGZ) via the type II systemJournal of Molecular Biology, 2000
- The C-terminal domain of the Pseudomonas secretin XcpQ forms oligomeric rings with pore activityJournal of Molecular Biology, 1999
- Bacterial Type II protein export and pilus biogenesis: more than just homologies?Trends in Cell Biology, 1999
- Assembly of the type II secretion machinery of Erwinia chrysanthemi: direct interaction and associated conformational change between OutE, the putative ATP-binding component and the membrane protein OutLJournal of Molecular Biology, 1999
- Mutual stabilization of the XcpZ and XcpY components of the secretory apparatus in Pseudomonas aeruginosaMicrobiology, 1998
- GSP-dependent protein secretion in Gram-negative bacteria: the Xcp system of Pseudomonas aeruginosaFEMS Microbiology Reviews, 1998
- The XcpR protein of Pseudomonas aeruginosa dimerizes via its N‐terminusMolecular Microbiology, 1997
- The extreme C-terminus is required for secretion of both the native polygalacturonase (PehA) and PehA-Bla hybrid proteins in Erwinia carotovora subsp. carotovoraMolecular Microbiology, 1995
- pIV, a Filamentous Phage Protein that Mediates Phage Export Across the Bacterial Cell Envelope, Forms a MultimerJournal of Molecular Biology, 1994
- Aeromonas spp. can secrete Escherichia coli alkaline phosphatase into the culture supernatant, and its release requires a functional general secretion pathwayMolecular Microbiology, 1993