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Composition and function of the DctA/DcuS sensor complex of E. coli

Subject Area Metabolism, Biochemistry and Genetics of Microorganisms
Term from 2015 to 2020
Project identifier Deutsche Forschungsgemeinschaft (DFG) - Project number 298847751
 
Final Report Year 2020

Final Report Abstract

Sensing of C4-DC by the DcuS-DcuR two-component system is remarkably complex and includes far-reaching complex formation by the sensors system. Function of DcuS requires interaction with transporters that convert DcuS to the sensory competent state. Under anaerobic conditions transporter DcuB serves as co-regulator, under aerobic conditions transporter DctA. The DctA-DcuS complex additionally interacts with the transporter DauA. The transporters, however, are not required for sensing which resides only in DcuS. The transporters DcuB and DctA rather convert DcuS to the C4-DC responsive state, whereas the role of DauA is obscure. The bacteria contain low levels of free (not-complexed) DcuSF. DcuSF is in the permanent active state and ensures basal level of DcuB synthesis in the absence of C4-DCs. DcuS forms a stable complex with DcuR with DcuR in vivo and in vitro which is further stabilized by phosphorylation of DcuS and of DcuR . Overall, the data imply that sensing by the DcuS-DcuR system is complex and requires complex formation with co-regulators representing transport proteins (DcuB, DctA, DauA). The mechanism behind the conversion of DcuS by the transporters to the C4-DC responsive state is still under study. Also, the physiological significance of co-regulation by the transport proteins has not become clear in all details. The closely related DcuA transporter that is a member of the Dcu family of transporters has no function in co-regulation of DcuS. DcuA functions as a L-aspartate/fumarate antiport and serves as a nitrogen shuttle for the net uptake of nitrogen (without net uptake of carbon).

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