Disease relevance of dppA

• Identification and characterization of dppA, an Escherichia coli gene encoding a periplasmic dipeptide transport protein [1].
• Contribution of dppA to urease activity in Helicobacter pylori 26695 [2].

High impact information on dppA

• The periplasmic dipeptide-binding protein (DBP), encoded by the dppA gene, also serves as a chemoreceptor [3].
• 0. The 310 nucleotides between dppA and dppB include a RIP (repetitive IHF-binding palindromic) element, whose deletion from a multi-copy plasmid causes fivefold and 10-fold reductions in the levels of upstream and downstream dpp mRNA, respectively [3].
• Transcription of the dpp operon initiates 165 bases upstream of the predicted dppA start codon [3].
• Downstream of dppA are other genes required for transport but not for chemotaxis [4].
• Genes encoding F1C fimbriae, both copies of P fimbriae, hemolysin, OmpF, a dipeptide transporter DppA, a heat shock chaperone IbpB, and clusters of open reading frames with unknown functions were also up-regulated [5].

Biological context of dppA

• The mutations, designated alu (ALA uptake), mapped to the 80-min region of the E. coli chromosome [6].

Associations of dppA with chemical compounds

• Insertional inactivation of dppA results in the inability of a proline auxotroph to utilize Pro-Gly as a proline source. dppA-dependent Pro-Gly utilization does not require any of the three major proline transport systems, demonstrating that DppA is not simply a dipeptidase [1].
• METHODS: A mutation in dppA, constructed by insertional inactivation with a chloramphenicol resistance cassette, was introduced by allelic exchange into H. pylori strain 26695 [2].

Regulatory relationships of dppA

• CONCLUSION: The results of this study indicate that the Y. pestis gcvB gene encodes two small non-coding regulatory RNAs that repress dppA expression [7].

References