Summary:
"Dihydroxyacetone Regulator," DhaR, is negatively autoregulated and coordinately activates transcription of the divergent dha operon (dhaKLM), which encodes three subunits of the dihydroxyacetone (DHA) kinase [1].
DhaR is inactivated when DnaK binds to the sensing domain of this regulator, in the absence of DHA [1]. Dephosphorylated DhaL (DhaL::ADP) is an antagonist of DhaK and also is able to form complexes with the sensing domain of DhaR. In the presence of DHA, DhaL::ADP displaces DhaK or blocks the association of the DhaK/DhaR complex and DhaR activates the transcription of the dha operon [1].
DhaR belongs to the family of bacterial enhancer-binding proteins which contain three domains: the sensing domain located in the N terminus, the central AAA+ domain, and the C-terminal domain, which contains a helix-turn-helix motif involved in the interaction with DNA. Although the C-terminal domain and the N-terminal domain from DhaR are similar to those of other members of this group, its central domain is not [1].
The central AAA+ domain does not contain the two conserved submotifs in this family (ESELF and GAFTGA) responsible for interaction with σ
54. As with other members of the family, the possibility exists that this regulator activates σ
70-dependent promoters instead of σ
54-dependent promoters
[1].
The crystal structure has been determined. DhaR regulates transcription by coiled-coil helix rotation, and this provides the mechanism for transmitting the binding signal from the GAF/PAS domains to the C-terminal DNA-binding domain
[].
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