ArticleProtein science : a publication of the Protein Society2008
Structure of AscE and induced burial regions in AscE and AscG upon formation of the chaperone needle-subunit complex of type III secretion system in Aeromonas hydrophila.
Article in Protein science : a publication of the Protein Society, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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10 citing papers in PubMed.
- Article
- An Update on the GenusMicroorganisms · 2020Review
- Chaperone-mediated secretion switching from early to middle substrates in the type III secretion system encoded byThe Journal of biological chemistry · 2019Article
- EscE and EscG are cochaperones for the type III needle protein EscF of enteropathogenic Escherichia coli.Journal of bacteriology · 2013Article
- Crystal structure of the heteromolecular chaperone, AscE-AscG, from the type III secretion system in Aeromonas hydrophila.PloS one · 2011Article
- Role of Hcp, a type 6 secretion system effector, of Aeromonas hydrophila in modulating activation of host immune cells.Microbiology (Reading, England) · 2010Article
- Protein refolding is required for assembly of the type three secretion needle.Nature structural & molecular biology · 2010Article
- Cochaperone interactions in export of the type III needle component PscF of Pseudomonas aeruginosa.Journal of bacteriology · 2010Article
- A dominant-negative needle mutant blocks type III secretion of early but not late substrates in Yersinia.Molecular microbiology · 2010Article
- Mapping of the chaperone AcrH binding regions of translocators AopB and AopD and characterization of oligomeric and metastable AcrH-AopB-AopD complexes in the type III secretion system of Aeromonas hydrophila.Protein science : a publication of the Protein Society · 2009Article
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Abstract
In the type III secretion system (T3SS) of Aeromonas hydrophila, the putative needle complex subunit AscF requires both putative chaperones AscE and AscG for formation of a ternary complex to avoid premature assembly. Here we report the crystal structure of AscE at 2.7 A resolution and the mapping of buried regions of AscE, AscG, and AscF in the AscEG and AscEFG complexes using limited protease digestion. The dimeric AscE is comprised of two helix-turn-helix monomers packed in an antiparallel fashion. The N-terminal 13 residues of AscE are buried only upon binding with AscG, but this region is found to be nonessential for the interaction. AscE functions as a monomer and can be coexpressed with AscG or with both AscG and AscF to form soluble complexes. The AscE binding region of AscG in the AscEG complex is identified to be within the N-terminal 61 residues of AscG. The exposed C-terminal substrate-binding region of AscG in the AscEG complex is induced to be buried only upon binding to AscF. However, the N-terminal 52 residues of AscF remain exposed even in the ternary AscEFG complex. On the other hand, the 35-residue C-terminal region of AscF in the complex is resistant to protease digestion in the AscEFG complex. Site-directed mutagenesis showed that two C-terminal hydrophobic residues, Ile83 and Leu84, of AscF are essential for chaperone binding.
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