Ligand binding analyses of the putative peptide transporter YjdL from E. coli display a significant selectivity towards dipeptides
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Proton-dependent oligopeptide transporters (POTs) are secondary active transporters that couple the inwards translocation of di- and tripeptides to inwards proton translocation. Escherichia coli contains four genes encoding the putative POT proteins YhiP, YdgR, YjdL and YbgH. We have over-expressed the previously uncharacterized YjdL and investigated the peptide specificity by means of uptake inhibition. The IC(50) value for the dipeptide Ala-Ala was measured to 22mM while Ala-Ala-Ala was not able to inhibit uptake. In addition, IC(50) values of 0.3mM and 1.5mM were observed for Ala-Lys and Tyr-Ala, respectively, while the alanyl-extended tripeptides Ala-Lys-Ala, Ala-Ala-Lys, Ala-Tyr-Ala and Tyr-Ala-Ala displayed values of 8, >50, 31 and 31mM, respectively. These results clearly indicate that unlike most POT members characterized to date, including YdgR and YhiP, YjdL shows significantly higher specificity towards dipeptides.
Originalsprog | Engelsk |
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Tidsskrift | Biochemical and Biophysical Research Communications |
Vol/bind | 389 |
Udgave nummer | 1 |
Sider (fra-til) | 112-116 |
ISSN | 0006-291X |
DOI | |
Status | Udgivet - 2009 |
- Det tidligere Farmaceutiske Fakultet
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ID: 14411038