PMID:15802652

Citation	Azim, MK, Goehring, W, Song, HK, Ramachandran, R, Bochtler, M and Goettig, P (2005) Characterization of the HslU chaperone affinity for HslV protease. Protein Sci. 14:1357-62
Abstract	The HslVU complex is a bacterial two-component ATP-dependent protease, consisting of HslU chaperone and HslV peptidase. Investigation of protein-protein interactions using SPR in Escherichia coli HslVU and the protein substrates demonstrates that HslU and HslV have moderate affinity (Kd = 1 microM) for each other. However, the affinity of HslU for HslV fivefold increased (Kd approximately 0.2 microM) after binding with the MBP approximately SulA protein indicating the formation of a "ternary complex" of HslV-HslU-MBP approximately SulA. The molecular interaction studies also revealed that HslU strongly binds to MBP approximately SulA with 10(-9) M affinity but does not associate with nonstructured casein. Conversely, HslV does not interact with the MBP-SulA whereas it strongly binds with casein (Kd = 0.2 microM) requiring an intact active site of HslV. These findings provide evidence for "substrate-induced" stable HslVU complex formation. Presumably, the binding of HslU to MBP approximately SulA stimulates a conformational change in HslU to a high-affinity form for HslV.
Links	PubMed PMC2253264 Online version:10.1110/ps.04970405
Keywords	Caseins/metabolism; Endopeptidase Clp/metabolism; Escherichia coli Proteins/metabolism; Substrate Specificity; Surface Plasmon Resonance
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