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

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New insights into the substrate specificities of proton-coupled oligopeptide transporters from E. coli by a pH sensitive assay. / Prabhala, Bala Krishna; Aduri, Nanda Gowtham; Jensen, Johanne Mørch; Ernst, Heidi Asschenfeldt; Iram, Nida; Rahman, Moazur; Mirza, Osman Asghar.

In: FEBS Letters, Vol. 588, No. 4, 16.01.2014, p. 560-565.

Research output: Contribution to journal › Journal article › Research › peer-review

Harvard

Prabhala, BK, Aduri, NG, Jensen, JM, Ernst, HA, Iram, N, Rahman, M & Mirza, OA 2014, 'New insights into the substrate specificities of proton-coupled oligopeptide transporters from E. coli by a pH sensitive assay', FEBS Letters, vol. 588, no. 4, pp. 560-565. https://doi.org/10.1016/j.febslet.2014.01.004

APA

Prabhala, B. K., Aduri, N. G., Jensen, J. M., Ernst, H. A., Iram, N., Rahman, M., & Mirza, O. A. (2014). New insights into the substrate specificities of proton-coupled oligopeptide transporters from E. coli by a pH sensitive assay. FEBS Letters, 588(4), 560-565. https://doi.org/10.1016/j.febslet.2014.01.004

Vancouver

Prabhala BK, Aduri NG, Jensen JM, Ernst HA, Iram N, Rahman M et al. New insights into the substrate specificities of proton-coupled oligopeptide transporters from E. coli by a pH sensitive assay. FEBS Letters. 2014 Jan 16;588(4):560-565. https://doi.org/10.1016/j.febslet.2014.01.004

Author

Prabhala, Bala Krishna ; Aduri, Nanda Gowtham ; Jensen, Johanne Mørch ; Ernst, Heidi Asschenfeldt ; Iram, Nida ; Rahman, Moazur ; Mirza, Osman Asghar. / New insights into the substrate specificities of proton-coupled oligopeptide transporters from E. coli by a pH sensitive assay. In: FEBS Letters. 2014 ; Vol. 588, No. 4. pp. 560-565.

Bibtex

@article{fb43a31906e142bc9bc9531caf16abd3,
title = "New insights into the substrate specificities of proton-coupled oligopeptide transporters from E. coli by a pH sensitive assay",
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 E. 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.",
author = "Prabhala, {Bala Krishna} and Aduri, {Nanda Gowtham} and Jensen, {Johanne M{\o}rch} and Ernst, {Heidi Asschenfeldt} and Nida Iram and Moazur Rahman and Mirza, {Osman Asghar}",
note = "Copyright {\textcopyright} 2014. Published by Elsevier B.V.",
year = "2014",
month = jan,
day = "16",
doi = "10.1016/j.febslet.2014.01.004",
language = "English",
volume = "588",
pages = "560--565",
journal = "F E B S Letters",
issn = "0014-5793",
publisher = "JohnWiley & Sons Ltd",
number = "4",

}

RIS

TY - JOUR

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

N1 - Copyright © 2014. Published by Elsevier B.V.

PY - 2014/1/16

Y1 - 2014/1/16

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 E. 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 E. 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

VL - 588

SP - 560

EP - 565

JO - F E B S Letters

JF - F E B S Letters

SN - 0014-5793

IS - 4

ER -

ID: 96234260