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Membrane Protein Activity Induces Specific Molecular Changes in Nanodiscs Monitored by FTIR Difference Spectroscopy

It is well known that lipids neighboring integral membrane proteins directly influence their function. The opposite effect is true as well, as membrane proteins undergo structural changes after activation and thus perturb the lipidic environment. Here, we studied the interaction between these molecu...

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Autores principales: Baserga, Federico, Vorkas, Antreas, Crea, Fucsia, Schubert, Luiz, Chen, Jheng-Liang, Redlich, Aoife, La Greca, Mariafrancesca, Storm, Julian, Oldemeyer, Sabine, Hoffmann, Kirsten, Schlesinger, Ramona, Heberle, Joachim
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Frontiers Media S.A. 2022
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9234331/
https://www.ncbi.nlm.nih.gov/pubmed/35769914
http://dx.doi.org/10.3389/fmolb.2022.915328
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author Baserga, Federico
Vorkas, Antreas
Crea, Fucsia
Schubert, Luiz
Chen, Jheng-Liang
Redlich, Aoife
La Greca, Mariafrancesca
Storm, Julian
Oldemeyer, Sabine
Hoffmann, Kirsten
Schlesinger, Ramona
Heberle, Joachim
author_facet Baserga, Federico
Vorkas, Antreas
Crea, Fucsia
Schubert, Luiz
Chen, Jheng-Liang
Redlich, Aoife
La Greca, Mariafrancesca
Storm, Julian
Oldemeyer, Sabine
Hoffmann, Kirsten
Schlesinger, Ramona
Heberle, Joachim
author_sort Baserga, Federico
collection PubMed
description It is well known that lipids neighboring integral membrane proteins directly influence their function. The opposite effect is true as well, as membrane proteins undergo structural changes after activation and thus perturb the lipidic environment. Here, we studied the interaction between these molecular machines and the lipid bilayer by observing changes in the lipid vibrational bands via FTIR spectroscopy. Membrane proteins with different functionalities have been reconstituted into lipid nanodiscs: Microbial rhodopsins that act as light-activated ion pumps (the proton pumps NsXeR and UmRh1, and the chloride pump NmHR) or as sensors (NpSRII), as well as the electron-driven cytochrome c oxidase RsCcO. The effects of the structural changes on the surrounding lipid phase are compared to mechanically induced lateral tension exerted by the light-activatable lipid analogue AzoPC. With the help of isotopologues, we show that the ν(C = O) ester band of the glycerol backbone reports on changes in the lipids’ collective state induced by mechanical changes in the transmembrane proteins. The perturbation of the nanodisc lipids seems to involve their phase and/or packing state. (13)C-labeling of the scaffold protein shows that its structure also responds to the mechanical expansion of the lipid bilayer.
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spelling pubmed-92343312022-06-28 Membrane Protein Activity Induces Specific Molecular Changes in Nanodiscs Monitored by FTIR Difference Spectroscopy Baserga, Federico Vorkas, Antreas Crea, Fucsia Schubert, Luiz Chen, Jheng-Liang Redlich, Aoife La Greca, Mariafrancesca Storm, Julian Oldemeyer, Sabine Hoffmann, Kirsten Schlesinger, Ramona Heberle, Joachim Front Mol Biosci Molecular Biosciences It is well known that lipids neighboring integral membrane proteins directly influence their function. The opposite effect is true as well, as membrane proteins undergo structural changes after activation and thus perturb the lipidic environment. Here, we studied the interaction between these molecular machines and the lipid bilayer by observing changes in the lipid vibrational bands via FTIR spectroscopy. Membrane proteins with different functionalities have been reconstituted into lipid nanodiscs: Microbial rhodopsins that act as light-activated ion pumps (the proton pumps NsXeR and UmRh1, and the chloride pump NmHR) or as sensors (NpSRII), as well as the electron-driven cytochrome c oxidase RsCcO. The effects of the structural changes on the surrounding lipid phase are compared to mechanically induced lateral tension exerted by the light-activatable lipid analogue AzoPC. With the help of isotopologues, we show that the ν(C = O) ester band of the glycerol backbone reports on changes in the lipids’ collective state induced by mechanical changes in the transmembrane proteins. The perturbation of the nanodisc lipids seems to involve their phase and/or packing state. (13)C-labeling of the scaffold protein shows that its structure also responds to the mechanical expansion of the lipid bilayer. Frontiers Media S.A. 2022-06-13 /pmc/articles/PMC9234331/ /pubmed/35769914 http://dx.doi.org/10.3389/fmolb.2022.915328 Text en Copyright © 2022 Baserga, Vorkas, Crea, Schubert, Chen, Redlich, La Greca, Storm, Oldemeyer, Hoffmann, Schlesinger and Heberle. https://creativecommons.org/licenses/by/4.0/This is an open-access article distributed under the terms of the Creative Commons Attribution License (CC BY). The use, distribution or reproduction in other forums is permitted, provided the original author(s) and the copyright owner(s) are credited and that the original publication in this journal is cited, in accordance with accepted academic practice. No use, distribution or reproduction is permitted which does not comply with these terms.
spellingShingle Molecular Biosciences
Baserga, Federico
Vorkas, Antreas
Crea, Fucsia
Schubert, Luiz
Chen, Jheng-Liang
Redlich, Aoife
La Greca, Mariafrancesca
Storm, Julian
Oldemeyer, Sabine
Hoffmann, Kirsten
Schlesinger, Ramona
Heberle, Joachim
Membrane Protein Activity Induces Specific Molecular Changes in Nanodiscs Monitored by FTIR Difference Spectroscopy
title Membrane Protein Activity Induces Specific Molecular Changes in Nanodiscs Monitored by FTIR Difference Spectroscopy
title_full Membrane Protein Activity Induces Specific Molecular Changes in Nanodiscs Monitored by FTIR Difference Spectroscopy
title_fullStr Membrane Protein Activity Induces Specific Molecular Changes in Nanodiscs Monitored by FTIR Difference Spectroscopy
title_full_unstemmed Membrane Protein Activity Induces Specific Molecular Changes in Nanodiscs Monitored by FTIR Difference Spectroscopy
title_short Membrane Protein Activity Induces Specific Molecular Changes in Nanodiscs Monitored by FTIR Difference Spectroscopy
title_sort membrane protein activity induces specific molecular changes in nanodiscs monitored by ftir difference spectroscopy
topic Molecular Biosciences
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9234331/
https://www.ncbi.nlm.nih.gov/pubmed/35769914
http://dx.doi.org/10.3389/fmolb.2022.915328
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