Curation Information

Publication
Integration of cyclic di-GMP and quorum sensing in the control of vpsT and aphA in Vibrio cholerae.;Srivastava D, Harris RC, Waters CM;Journal of bacteriology 2011 Nov; 193(22):6331-41 [21926235]
TF
HapR [A0A0H3Q915, view regulon]
Reported TF sp.
Vibrio cholerae O1 biovar El Tor str. C6706
Reported site sp.
Vibrio cholerae O1 biovar El Tor str. C6706
Created by
Erill Lab
Curation notes
-

Experimental Process

The vpsT and aphA promoters were shown to be inducible with c-di-GMP using lux assays. Sites for Lrp, HapR and VpsR were predicted by comparison to known consensus. The transcriptional start site of vpsT was determined with RACE PCR. EMSAs with multiple size fragments confirmed that the VpsR sites were located upstream of -119 from TSS. Expression assays with vpsR and hapR mutants using multiple size fragments also showed that it they are required for induction of both promoters and that the predicted sites are likely responsible for such induction.

Transcription Factor Binding Sites


TATTGAGAATAATGTCAGTTT
TATTGATATTCTTAATATTGA
TATTGAGAATAATGTCAGTTT
TATTGATATTCTTAATATTGA

Gene Regulation

Regulated genes for each binding site are displayed below. Gene regulation diagrams show binding sites, positively-regulated genes, negatively-regulated genes, both positively and negatively regulated genes, genes with unspecified type of regulation. For each indvidual site, experimental techniques used to determine the site are also given.

Site sequence Regulated genes Gene diagram Experimental techniques TF function TF type
TATTGAGAATAATGTCAGTTT VCD_001716
... ... VCD_001716
Experimental technique details Consensus search (ECO:0005624) - Experimental technique details Luciferase reporter assay (ECO:0005648) - repressor monomer
TATTGATATTCTTAATATTGA VCD_000383,
... ... VCD_000383 VCD_000382
Experimental technique details Consensus search (ECO:0005624) - Experimental technique details EMSA (ECO:0001807) - Experimental technique details Luciferase reporter assay (ECO:0005648) - repressor monomer