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

Johanne M Jensen; Nanda Gowtham Aduri; Bala K Prabhala; Rasmus Jahnsen; Henrik Franzyk; Osman Asghar Mirza

doi:10.1016/j.biocel.2014.09.016

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

Johanne M Jensen, Nanda Gowtham Aduri, Bala K Prabhala, Rasmus Jahnsen, Henrik Franzyk, Osman Asghar Mirza

5 Citations (Scopus)

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.

Original language	English
Journal	International Journal of Biochemistry & Cell Biology
Volume	55
Pages (from-to)	311-17
Number of pages	7
ISSN	1357-2725
DOIs	https://doi.org/10.1016/j.biocel.2014.09.016
Publication status	Published - Oct 2014

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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 et al.
In: International Journal of Biochemistry & Cell Biology, Vol. 55, 10.2014, p. 311-17.

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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.",

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doi = "10.1016/j.biocel.2014.09.016",

language = "English",

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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

PY - 2014/10

Y1 - 2014/10

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

SN - 1357-2725

VL - 55

SP - 311

EP - 317

JO - International Journal of Biochemistry & Cell Biology

JF - International Journal of Biochemistry & Cell Biology

ER -

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

Abstract

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