Critical role of a conserved transmembrane lysine in substrate recognition by the proton-coupled oligopeptide transporter YjdL

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

Standard

Critical role of a conserved transmembrane lysine in substrate recognition by the proton-coupled oligopeptide transporter YjdL. / Jensen, Johanne M; Aduri, Nanda Gowtham; Prabhala, Bala K; Jahnsen, Rasmus; Franzyk, Henrik; Mirza, Osman Asghar.

In: International Journal of Biochemistry & Cell Biology, Vol. 55, 24.09.2014, p. 311-17.

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

Harvard

Jensen, JM, Aduri, NG, Prabhala, BK, Jahnsen, R, Franzyk, H & Mirza, OA 2014, 'Critical role of a conserved transmembrane lysine in substrate recognition by the proton-coupled oligopeptide transporter YjdL', International Journal of Biochemistry & Cell Biology, vol. 55, pp. 311-17. https://doi.org/10.1016/j.biocel.2014.09.016

APA

Jensen, J. M., Aduri, N. G., Prabhala, B. K., Jahnsen, R., Franzyk, H., & Mirza, O. A. (2014). Critical role of a conserved transmembrane lysine in substrate recognition by the proton-coupled oligopeptide transporter YjdL. International Journal of Biochemistry & Cell Biology, 55, 311-17. https://doi.org/10.1016/j.biocel.2014.09.016

Vancouver

Jensen JM, Aduri NG, Prabhala BK, Jahnsen R, Franzyk H, Mirza OA. Critical role of a conserved transmembrane lysine in substrate recognition by the proton-coupled oligopeptide transporter YjdL. International Journal of Biochemistry & Cell Biology. 2014 Sep 24;55:311-17. https://doi.org/10.1016/j.biocel.2014.09.016

Author

Jensen, Johanne M ; Aduri, Nanda Gowtham ; Prabhala, Bala K ; Jahnsen, Rasmus ; Franzyk, Henrik ; Mirza, Osman Asghar. / Critical role of a conserved transmembrane lysine in substrate recognition by the proton-coupled oligopeptide transporter YjdL. In: International Journal of Biochemistry & Cell Biology. 2014 ; Vol. 55. pp. 311-17.

Bibtex

@article{a12701defe9844829ddf584208f2a4e9,
title = "Critical role of a conserved transmembrane lysine in substrate recognition by the proton-coupled oligopeptide transporter YjdL",
abstract = "Proton-coupled oligopeptide transporters (POTs) utilize an electrochemical proton gradient to accumulate peptides in the cytoplasm. Changing the highly conserved active-site Lys117 in the Escherichia coli POT YjdL to glutamine resulted in loss of ligand affinity as well as inability to distinguish between a dipeptide ligand and the corresponding dipeptide amide. The radically changed pHBulk profiles of Lys117Gln and Lys117Arg mutants indicate an important role of Lys117 in facilitating protonation of the transporter; a notion that is supported by the close proximity of Lys117 to the conserved ExxERFxYY POT motif previously shown to be involved in proton translocation. These results point toward a novel dual role of Lys117 in direct or indirect interaction with both proton and peptide.",
author = "Jensen, {Johanne M} and Aduri, {Nanda Gowtham} and Prabhala, {Bala K} and Rasmus Jahnsen and Henrik Franzyk and Mirza, {Osman Asghar}",
note = "Copyright {\textcopyright} 2014. Published by Elsevier Ltd.",
year = "2014",
month = sep,
day = "24",
doi = "10.1016/j.biocel.2014.09.016",
language = "English",
volume = "55",
pages = "311--17",
journal = "International Journal of Biochemistry & Cell Biology",
issn = "1357-2725",
publisher = "Elsevier",

}

RIS

TY - JOUR

T1 - Critical role of a conserved transmembrane lysine in substrate recognition by the proton-coupled oligopeptide transporter YjdL

AU - Jensen, Johanne M

AU - Aduri, Nanda Gowtham

AU - Prabhala, Bala K

AU - Jahnsen, Rasmus

AU - Franzyk, Henrik

AU - Mirza, Osman Asghar

N1 - Copyright © 2014. Published by Elsevier Ltd.

PY - 2014/9/24

Y1 - 2014/9/24

N2 - Proton-coupled oligopeptide transporters (POTs) utilize an electrochemical proton gradient to accumulate peptides in the cytoplasm. Changing the highly conserved active-site Lys117 in the Escherichia coli POT YjdL to glutamine resulted in loss of ligand affinity as well as inability to distinguish between a dipeptide ligand and the corresponding dipeptide amide. The radically changed pHBulk profiles of Lys117Gln and Lys117Arg mutants indicate an important role of Lys117 in facilitating protonation of the transporter; a notion that is supported by the close proximity of Lys117 to the conserved ExxERFxYY POT motif previously shown to be involved in proton translocation. These results point toward a novel dual role of Lys117 in direct or indirect interaction with both proton and peptide.

AB - Proton-coupled oligopeptide transporters (POTs) utilize an electrochemical proton gradient to accumulate peptides in the cytoplasm. Changing the highly conserved active-site Lys117 in the Escherichia coli POT YjdL to glutamine resulted in loss of ligand affinity as well as inability to distinguish between a dipeptide ligand and the corresponding dipeptide amide. The radically changed pHBulk profiles of Lys117Gln and Lys117Arg mutants indicate an important role of Lys117 in facilitating protonation of the transporter; a notion that is supported by the close proximity of Lys117 to the conserved ExxERFxYY POT motif previously shown to be involved in proton translocation. These results point toward a novel dual role of Lys117 in direct or indirect interaction with both proton and peptide.

U2 - 10.1016/j.biocel.2014.09.016

DO - 10.1016/j.biocel.2014.09.016

M3 - Journal article

C2 - 25261786

VL - 55

SP - 311

EP - 317

JO - International Journal of Biochemistry & Cell Biology

JF - International Journal of Biochemistry & Cell Biology

SN - 1357-2725

ER -

ID: 124336908