| Structural biology of type VI secretion systems. | |
| | |
MedLine Citation:
|
PMID: 22411981 Owner: NLM Status: MEDLINE |
Abstract/OtherAbstract:
|
Type VI secretion systems (T6SSs) are transenvelope complexes specialized in the transport of proteins or domains directly into target cells. These systems are versatile as they can target either eukaryotic host cells and therefore modulate the bacteria-host interaction and pathogenesis or bacterial cells and therefore facilitate access to a specific niche. These molecular machines comprise at least 13 proteins. Although recent years have witnessed advances in the role and function of these secretion systems, little is known about how these complexes assemble in the cell envelope. Interestingly, the current information converges to the idea that T6SSs are composed of two subassemblies, one resembling the contractile bacteriophage tail, whereas the other subunits are embedded in the inner and outer membranes and anchor the bacteriophage-like structure to the cell envelope. In this review, we summarize recent structural information on individual T6SS components emphasizing the fact that T6SSs are composite systems, adapting subunits from various origins. |
| | |
Authors:
|
Eric Cascales; Christian Cambillau |
Publication Detail:
|
Type: Journal Article; Research Support, Non-U.S. Gov't; Review |
Journal Detail:
|
Title: Philosophical transactions of the Royal Society of London. Series B, Biological sciences Volume: 367 ISSN: 1471-2970 ISO Abbreviation: Philos. Trans. R. Soc. Lond., B, Biol. Sci. Publication Date: 2012 Apr |
Date Detail:
|
Created Date: 2012-03-13 Completed Date: 2012-06-26 Revised Date: 2013-05-20 |
Medline Journal Info:
|
Nlm Unique ID: 7503623 Medline TA: Philos Trans R Soc Lond B Biol Sci Country: England |
Other Details:
|
Languages: eng Pagination: 1102-11 Citation Subset: IM |
Affiliation:
|
CNRS, Laboratoire d'Ingénierie des Systèmes Macromoléculaires, UMR 7255, Institut de Microbiologie de la Méditerranée, Aix-Marseille Université, 31 Chemin Joseph Aiguier, 13402 Marseille Cedex 20, France. cascales@imm.cnrs.fr |
Export Citation:
|
APA/MLA Format Download EndNote Download BibTex |
| MeSH Terms | |
Descriptor/Qualifier:
|
Bacterial Proteins
/
chemistry* Bacterial Secretion Systems* Cell Membrane / chemistry Escherichia coli / chemistry Escherichia coli Proteins / chemistry Lipopeptides / chemistry Membrane Proteins / chemistry Models, Molecular Molecular Chaperones / chemistry Multiprotein Complexes / chemistry* Periplasm / chemistry Protein Folding Protein Structure, Tertiary Protein Transport |
| Chemical | |
Reg. No./Substance:
|
0/Bacterial Proteins; 0/Escherichia coli Proteins; 0/Lipopeptides; 0/Membrane Proteins; 0/Molecular Chaperones; 0/Multiprotein Complexes; 0/TssJ protein, E coli |
| Comments/Corrections | |
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine
Previous Document: Type V secretion: mechanism(s) of autotransport through the bacterial outer membrane.
Next Document: Chaperone-usher pathways: diversity and pilus assembly mechanism.