Please use this identifier to cite or link to this item: https://doi.org/10.1002/pro.187
Title: 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
Authors: Yih, W.T.
Hong, B.Y. 
Sivaraman, J. 
Ka, Y.L. 
Mok, Y.-K. 
Keywords: Chaperone AcrH
Coexpression
Oligomerization
Translocators AopB and AopD
Type III secretion system
Issue Date: Aug-2009
Source: Yih, W.T., Hong, B.Y., Sivaraman, J., Ka, Y.L., Mok, Y.-K. (2009-08). 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 18 (8) : 1724-1734. ScholarBank@NUS Repository. https://doi.org/10.1002/pro.187
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. © 2009 The Protein Society.
Source Title: Protein Science
URI: http://scholarbank.nus.edu.sg/handle/10635/101055
ISSN: 09618368
DOI: 10.1002/pro.187
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