New insights into the substrate specificities of proton-coupled oligopeptide transporters from E. coli by a pH sensitive assay

Bala Krishna Prabhala; Nanda Gowtham Aduri; Johanne Mørch Jensen; Heidi Asschenfeldt Ernst; Nida Iram; Moazur Rahman; Osman Asghar Mirza

doi:10.1016/j.febslet.2014.01.004

New insights into the substrate specificities of proton-coupled oligopeptide transporters from E. coli by a pH sensitive assay

Bala Krishna Prabhala, Nanda Gowtham Aduri, Johanne Mørch Jensen, Heidi Asschenfeldt Ernst, Nida Iram, Moazur Rahman, Osman Asghar Mirza

14 Citationer (Scopus)

Abstract

Proton-coupled oligopeptide transporters (POTs) are secondary active transporters that facilitate di- and tripeptide uptake by coupling it to an inward directed proton electrochemical gradient. Here the substrate specificities of Escherichia coli POTs YdgR, YhiP and YjdL were investigated by means of a label free transport assay using the hydrophilic pH sensitive dye pyranine and POT overexpressing E. coli cells. The results confirm and extend the functional knowledge on E. coli POTs. In contrast to previous assumptions, alanine and trialanine appears to be substrates of YjdL, albeit poor compared to dipeptides. Similarly tetraalanine apparently is a substrate of both YdgR and YhiP.

Originalsprog	Engelsk
Tidsskrift	FEBS Letters
Vol/bind	588
Udgave nummer	4
Sider (fra-til)	560-565
ISSN	0014-5793
DOI	https://doi.org/10.1016/j.febslet.2014.01.004
Status	Udgivet - 14 feb. 2014

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10.1016/j.febslet.2014.01.004

https://febs.onlinelibrary.wiley.com/doi/pdfdirect/10.1016/j.febslet.2014.01.004

Citationsformater

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abstract = "Proton-coupled oligopeptide transporters (POTs) are secondary active transporters that facilitate di- and tripeptide uptake by coupling it to an inward directed proton electrochemical gradient. Here the substrate specificities of Escherichia coli POTs YdgR, YhiP and YjdL were investigated by means of a label free transport assay using the hydrophilic pH sensitive dye pyranine and POT overexpressing E. coli cells. The results confirm and extend the functional knowledge on E. coli POTs. In contrast to previous assumptions, alanine and trialanine appears to be substrates of YjdL, albeit poor compared to dipeptides. Similarly tetraalanine apparently is a substrate of both YdgR and YhiP.",

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T1 - New insights into the substrate specificities of proton-coupled oligopeptide transporters from E. coli by a pH sensitive assay

AU - Prabhala, Bala Krishna

AU - Aduri, Nanda Gowtham

AU - Jensen, Johanne Mørch

AU - Ernst, Heidi Asschenfeldt

AU - Iram, Nida

AU - Rahman, Moazur

AU - Mirza, Osman Asghar

PY - 2014/2/14

Y1 - 2014/2/14

N2 - Proton-coupled oligopeptide transporters (POTs) are secondary active transporters that facilitate di- and tripeptide uptake by coupling it to an inward directed proton electrochemical gradient. Here the substrate specificities of Escherichia coli POTs YdgR, YhiP and YjdL were investigated by means of a label free transport assay using the hydrophilic pH sensitive dye pyranine and POT overexpressing E. coli cells. The results confirm and extend the functional knowledge on E. coli POTs. In contrast to previous assumptions, alanine and trialanine appears to be substrates of YjdL, albeit poor compared to dipeptides. Similarly tetraalanine apparently is a substrate of both YdgR and YhiP.

AB - Proton-coupled oligopeptide transporters (POTs) are secondary active transporters that facilitate di- and tripeptide uptake by coupling it to an inward directed proton electrochemical gradient. Here the substrate specificities of Escherichia coli POTs YdgR, YhiP and YjdL were investigated by means of a label free transport assay using the hydrophilic pH sensitive dye pyranine and POT overexpressing E. coli cells. The results confirm and extend the functional knowledge on E. coli POTs. In contrast to previous assumptions, alanine and trialanine appears to be substrates of YjdL, albeit poor compared to dipeptides. Similarly tetraalanine apparently is a substrate of both YdgR and YhiP.

U2 - 10.1016/j.febslet.2014.01.004

DO - 10.1016/j.febslet.2014.01.004

M3 - Journal article

C2 - 24440353

SN - 0014-5793

VL - 588

SP - 560

EP - 565

JO - F E B S Letters

JF - F E B S Letters

IS - 4

ER -

New insights into the substrate specificities of proton-coupled oligopeptide transporters from E. coli by a pH sensitive assay

Abstract

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