NDLI: DNA Interaction and Phosphotransfer of the C4-Dicarboxylate- Responsive DcuS-DcuR Two-Component Regulatory System from Escherichia coli

Content Provider	PubMed Central
Author	Abo-amer, Aly E. Munn, Jonathan Jackson, Kerry Aktas, Murat Golby, Paul Kelly, David J. Andrews, Simon C.
Copyright Year	2004
Abstract	The DcuS-DcuR system of Escherichia coli is a two-component sensor-regulator that controls gene expression in response to external C4-dicarboxylates and citrate. The DcuS protein is particularly interesting since it contains two PAS domains, namely a periplasmic C4-dicarboxylate-sensing PAS domain (PASp) and a cytosolic PAS domain (PASc) of uncertain function. For a study of the role of the PASc domain, three different fragments of DcuS were overproduced and examined: they were PASc-kinase, PASc, and kinase. The two kinase-domain-containing fragments were autophosphorylated by [γ-32P]ATP. The rate was not affected by fumarate or succinate, supporting the role of the PASp domain in C4-dicarboxylate sensing. Both of the phosphorylated DcuS constructs were able to rapidly pass their phosphoryl groups to DcuR, and after phosphorylation, DcuR dephosphorylated rapidly. No prosthetic group or significant quantity of metal was found associated with either of the PASc-containing proteins. The DNA-binding specificity of DcuR was studied by use of the pure protein. It was found to be converted from a monomer to a dimer upon acetylphosphate treatment, and native polyacrylamide gel electrophoresis suggested that it can oligomerize. DcuR specifically bound to the promoters of the three known DcuSR-regulated genes (dctA, dcuB, and frdA), with apparent KD s of 6 to 32 μM for untreated DcuR and ≤1 to 2 μM for the acetylphosphate-treated form. The binding sites were located by DNase I footprinting, allowing a putative DcuR-binding motif [tandemly repeated (T/A)(A/T)(T/C)(A/T)AA sequences] to be identified. The DcuR-binding sites of the dcuB, dctA, and frdA genes were located 27, 94, and 86 bp, respectively, upstream of the corresponding +1 sites, and a new promoter was identified for dcuB that responds to DcuR.
Related Links	http://dx.doi.org/10.1128/jb.186.6.1879-1889.2004
Ending Page	1889
Page Count	11
Starting Page	1879
File Format	PDF
ISSN	00219193
e-ISSN	10985530
Journal	Journal of Bacteriology
Issue Number	6
Volume Number	186
Language	English
Publisher	American Society for Microbiology
Publisher Date	2004-03-15
Access Restriction	Open
Rights Holder	American Society for Microbiology
Subject Keyword	Molecular Biology Microbiology Research in Higher Education
Content Type	Text
Resource Type	Article
Subject	Molecular Biology Microbiology

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