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A Loose Relationship: Incomplete H(+)/Sugar Coupling in the MFS Sugar Transporter GlcP

The glucose transporter from Staphylococcus epidermidis, GlcP(Se), is a homolog of the human GLUT sugar transporters of the major facilitator superfamily. Together with the xylose transporter from Escherichia coli, XylE(Ec), the other prominent prokaryotic GLUT homolog, GlcP(Se), is equipped with a...

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Autores principales: Bazzone, Andre, Zabadne, Annas J., Salisowski, Anastasia, Madej, M. Gregor, Fendler, Klaus
Formato: Online Artículo Texto
Lenguaje:English
Publicado: The Biophysical Society 2017
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5770559/
https://www.ncbi.nlm.nih.gov/pubmed/29262366
http://dx.doi.org/10.1016/j.bpj.2017.09.038
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author Bazzone, Andre
Zabadne, Annas J.
Salisowski, Anastasia
Madej, M. Gregor
Fendler, Klaus
author_facet Bazzone, Andre
Zabadne, Annas J.
Salisowski, Anastasia
Madej, M. Gregor
Fendler, Klaus
author_sort Bazzone, Andre
collection PubMed
description The glucose transporter from Staphylococcus epidermidis, GlcP(Se), is a homolog of the human GLUT sugar transporters of the major facilitator superfamily. Together with the xylose transporter from Escherichia coli, XylE(Ec), the other prominent prokaryotic GLUT homolog, GlcP(Se), is equipped with a conserved proton-binding site arguing for an electrogenic transport mode. However, the electrophysiological analysis of GlcP(Se) presented here reveals important differences between the two GLUT homologs. GlcP(Se), unlike XylE(Ec), does not perform steady-state electrogenic transport at symmetrical pH conditions. Furthermore, when a pH gradient is applied, partially uncoupled transport modes can be generated. In contrast to other bacterial sugar transporters analyzed so far, in GlcP(Se) sugar binding, translocation and release are also accomplished by the deprotonated transporter. Based on these experimental results, we conclude that coupling of sugar and H(+) transport is incomplete in GlcP(Se). To verify the viability of the observed partially coupled GlcP(Se) transport modes, we propose a universal eight-state kinetic model in which any degree of coupling is realized and H(+)/sugar symport represents only a specific instance. Furthermore, using sequence comparison with strictly coupled XylE(Ec) and similar sugar transporters, we identify an additional charged residue that may be essential for effective H(+)/sugar symport.
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spelling pubmed-57705592018-12-19 A Loose Relationship: Incomplete H(+)/Sugar Coupling in the MFS Sugar Transporter GlcP Bazzone, Andre Zabadne, Annas J. Salisowski, Anastasia Madej, M. Gregor Fendler, Klaus Biophys J Channels and Transporters The glucose transporter from Staphylococcus epidermidis, GlcP(Se), is a homolog of the human GLUT sugar transporters of the major facilitator superfamily. Together with the xylose transporter from Escherichia coli, XylE(Ec), the other prominent prokaryotic GLUT homolog, GlcP(Se), is equipped with a conserved proton-binding site arguing for an electrogenic transport mode. However, the electrophysiological analysis of GlcP(Se) presented here reveals important differences between the two GLUT homologs. GlcP(Se), unlike XylE(Ec), does not perform steady-state electrogenic transport at symmetrical pH conditions. Furthermore, when a pH gradient is applied, partially uncoupled transport modes can be generated. In contrast to other bacterial sugar transporters analyzed so far, in GlcP(Se) sugar binding, translocation and release are also accomplished by the deprotonated transporter. Based on these experimental results, we conclude that coupling of sugar and H(+) transport is incomplete in GlcP(Se). To verify the viability of the observed partially coupled GlcP(Se) transport modes, we propose a universal eight-state kinetic model in which any degree of coupling is realized and H(+)/sugar symport represents only a specific instance. Furthermore, using sequence comparison with strictly coupled XylE(Ec) and similar sugar transporters, we identify an additional charged residue that may be essential for effective H(+)/sugar symport. The Biophysical Society 2017-12-19 2017-12-19 /pmc/articles/PMC5770559/ /pubmed/29262366 http://dx.doi.org/10.1016/j.bpj.2017.09.038 Text en © 2017 Biophysical Society. http://creativecommons.org/licenses/by-nc-nd/4.0/ This is an open access article under the CC BY-NC-ND license (http://creativecommons.org/licenses/by-nc-nd/4.0/).
spellingShingle Channels and Transporters
Bazzone, Andre
Zabadne, Annas J.
Salisowski, Anastasia
Madej, M. Gregor
Fendler, Klaus
A Loose Relationship: Incomplete H(+)/Sugar Coupling in the MFS Sugar Transporter GlcP
title A Loose Relationship: Incomplete H(+)/Sugar Coupling in the MFS Sugar Transporter GlcP
title_full A Loose Relationship: Incomplete H(+)/Sugar Coupling in the MFS Sugar Transporter GlcP
title_fullStr A Loose Relationship: Incomplete H(+)/Sugar Coupling in the MFS Sugar Transporter GlcP
title_full_unstemmed A Loose Relationship: Incomplete H(+)/Sugar Coupling in the MFS Sugar Transporter GlcP
title_short A Loose Relationship: Incomplete H(+)/Sugar Coupling in the MFS Sugar Transporter GlcP
title_sort loose relationship: incomplete h(+)/sugar coupling in the mfs sugar transporter glcp
topic Channels and Transporters
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5770559/
https://www.ncbi.nlm.nih.gov/pubmed/29262366
http://dx.doi.org/10.1016/j.bpj.2017.09.038
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