ArticleProtein science : a publication of the Protein Society2009
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.
Article in Protein science : a publication of the Protein Society, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.
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13 citing papers in PubMed.
- Type III secretion system chaperones: a helping hand for secretion.Microbiology (Reading, England) · 2026Review
- Class II chaperones: indispensable components of the Gram-negative bacterial T3SS as guardians of translocators.Archives of microbiology · 2026Review
- Exploring the "N-Terminal Anchor" Binding Interface of the T3SS Chaperone-Translocator Complexes fromBiochemistry · 2023Article
- Evolutionary Conservation, Variability, and Adaptation of Type III Secretion Systems.The Journal of membrane biology · 2022Review
- Virulence Factors of Aeromonas hydrophila: In the Wake of Reclassification.Frontiers in microbiology · 2016Review
- LcrH, a class II chaperone from the type three secretion system, has a highly flexible native structure.The Journal of biological chemistry · 2013Article
- A translocator-specific export signal establishes the translocator-effector secretion hierarchy that is important for type III secretion system function.Molecular microbiology · 2012Article
- YspC: a unique translocator exhibits structural alteration in the complex form with chaperone SycB.The protein journal · 2012Article
- Crystal structure of the Yersinia enterocolitica type III secretion chaperone SycD in complex with a peptide of the minor translocator YopD.BMC structural biology · 2012Article
- Characterization of molten globule PopB in absence and presence of its chaperone PcrH.The protein journal · 2012Article
- Expression, purification, structural and functional analysis of SycB: a type three secretion chaperone from Yersinia enterocolitica.The protein journal · 2012Article
- Efficient isolation of Pseudomonas aeruginosa type III secretion translocators and assembly of heteromeric transmembrane pores in model membranes.Biochemistry · 2011Article
- Crystal structure of the heteromolecular chaperone, AscE-AscG, from the type III secretion system in Aeromonas hydrophila.PloS one · 2011Article
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5 authors.
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Abstract
In the type III secretion system (T3SS) of Aeromonas hydrophila, AcrH acts as a chaperone for translocators AopB and AopD. AcrH forms a stable 1:1 monomeric complex with AopD, whereas the 1:1 AcrH-AopB complex exists mainly as a metastable oligomeric form and only in minor amounts as a stable monomeric form. Limited protease digestion shows that these complexes contain highly exposed regions, thus allowing mapping of intact functional chaperone binding regions of AopB and AopD. AopD uses the transmembrane domain (DF1, residues 16-147) and the C-terminal amphipathic helical domain (DF2, residues 242-296) whereas AopB uses a discrete region containing the transmembrane domain and the putative N-terminal coiled coil domain (BF1, residues 33-264). Oligomerization of the AcrH-AopB complex is mainly through the C-terminal coiled coil domain of AopB, which is dispensable for chaperone binding. The three proteins, AcrH, AopB, and AopD, can be coexpressed to form an oligomeric and metastable complex. These three proteins are also oligomerized mainly through the C-terminal domain of AopB. Formation of such an oligomeric and metastable complex may be important for the proper formation of translocon of correct topology and stoichiometry on the host membrane.
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