Getting out: protein traffic in prokaryotes
- 8 March 2004
- journal article
- review article
- Published by Wiley in Molecular Microbiology
- Vol. 52 (1) , 3-11
- https://doi.org/10.1111/j.1365-2958.2003.03966.x
Abstract
Summary Protein secretion systems in prokaryotes are increas- ingly shifting from being considered as experimental models for 'more complex' processes (i.e. eukary- otes) to being a major source of key biological ques- tions in their own right. The pathways by which proteins move between compartments or insert into membranes in prokaryotic cells are certainly less numerous than in eukaryotes (though not dramati- cally so). However, the quality and complexity of bac- terial protein targeting systems indicate that virtually all mechanistic problems associated with protein traf- fic were solved very efficiently well before eukaryotes appeared on the Earth crust. Indeed, recent studies have both increased the number of known prokaryotic protein traffic systems and indicated new layers of complexity for those that were already well character- ized. This report describes some recent develop- ments in bacterial protein traffic that were presented at two meetings in the autumn of 2003.Keywords
This publication has 30 references indexed in Scilit:
- Bacterial shapeMolecular Microbiology, 2003
- Role of a Highly Conserved Bacterial Protein in Outer Membrane Protein AssemblyScience, 2003
- Chaperone Priming of Pilus Subunits Facilitates a Topological Transition that Drives Fiber FormationCell, 2002
- Shigella Spa32 Is an Essential Secretory Protein for Functional Type III Secretion Machinery and Uniformity of Its Needle LengthJournal of Bacteriology, 2002
- Architecture of the Protein-Conducting Channel Associated with the Translating 80S RibosomeCell, 2001
- Mapping the Sites of Interaction between SecY and SecE by Cysteine Scanning MutagenesisPublished by Elsevier ,2001
- Two‐partner secretion in Gram‐negative bacteria: a thrifty, specific pathway for large virulence proteinsMolecular Microbiology, 2001
- Translocase-Bound SecA Is Largely Shielded from the Phospholipid Acyl ChainsBiochemistry, 1998
- The Aqueous Pore through the Translocon Has a Diameter of 40–60 Å during Cotranslational Protein Translocation at the ER MembraneCell, 1997
- SecE‐dependent overproduction of SecY in Escherichia coliFEBS Letters, 1990