Disease relevance of aphA

• Overexpression of HapR also reduced aphA expression in both C6706 and Escherichia coli [1].
• Regulation of virulence gene expression in Vibrio cholerae by quorum sensing: HapR functions at the aphA promoter [1].
• This extends over the N-terminal 100 residues of bacteriophage phosphatases and E. coli diadenosine tetraphosphatase [2].

High impact information on aphA

• We show here that HapR influences the virulence cascade by directly repressing aphA expression [1].
• We previously reported that the Escherichia coli drug-resistance determinants aphA (kanamycin-resistance) and cat (chloramphenicol-resistance) could be introduced to Deinococcus radiodurans by transformation methods that produce duplication insertion [3].
• A clone overproducing diadenosine tetraphosphatase (diadenosine 5', 5'''-P1, P4-tetraphosphate pyrophosphohydrolase) activity was isolated from an Escherichia coli cosmid library [4].
• Conservation analysis and structure prediction of the protein serine/threonine phosphatases. Sequence similarity with diadenosine tetraphosphatase from Escherichia coli suggests homology to the protein phosphatases [2].
• The gene for Escherichia coli diadenosine tetraphosphatase is located immediately clockwise to folA and forms an operon with ksgA [5].

Biological context of aphA

• The gene conferring resistance to kanamycin, aphA, and originating from the streptococcal plasmid pJH1 was inserted into a shuttle vector [6].
• The starting point for aphA transcription, determined by S1 nuclease mapping, was located 340 base pairs upstream from the ATG translational initiator codon [6].

References