The non-bilayer lipid MGDG stabilizes the major light-harvesting complex (LHCII) against unfolding

Abstract In the photosynthetic apparatus of plants a high proportion of LHCII protein is needed to integrate 50% non-bilayer lipid MGDG into the lamellar thylakoid membrane, but whether and how the stability of the protein is also affected is not known. Here we use single-molecule force spectroscopy...

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Autores principales:	Dennis Seiwert, Hannes Witt, Andreas Janshoff, Harald Paulsen
Formato:	article
Lenguaje:	EN
Publicado:	Nature Portfolio 2017
Materias:	Medicine R Science Q
Acceso en línea:	https://doaj.org/article/36d83c49dce9466c82514e87ffab3aed
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spelling	oai:doaj.org-article:36d83c49dce9466c82514e87ffab3aed2021-12-02T12:32:05ZThe non-bilayer lipid MGDG stabilizes the major light-harvesting complex (LHCII) against unfolding10.1038/s41598-017-05328-72045-2322https://doaj.org/article/36d83c49dce9466c82514e87ffab3aed2017-07-01T00:00:00Zhttps://doi.org/10.1038/s41598-017-05328-7https://doaj.org/toc/2045-2322Abstract In the photosynthetic apparatus of plants a high proportion of LHCII protein is needed to integrate 50% non-bilayer lipid MGDG into the lamellar thylakoid membrane, but whether and how the stability of the protein is also affected is not known. Here we use single-molecule force spectroscopy to map the stability of LHCII against mechanical unfolding along the polypeptide chain as a function of oligomerization state and lipid composition. Comparing unfolding forces between monomeric and trimeric LHCII demonstrates that the stability does not increase significantly upon trimerization but can mainly be correlated with specific contact sites between adjacent monomers. In contrast, unfolding of trimeric complexes in membranes composed of different thylakoid lipids reveals that the non-bilayer lipid MGDG substantially increases the mechanical stability of LHCII in many segments of the protein compared to other lipids such as DGDG or POPG. We attribute these findings to steric matching of conically formed MGDG and the hourglass shape of trimeric LHCII, thereby extending the role of non-bilayer lipids to the structural stabilization of membrane proteins in addition to the modulation of their folding, conformation and function.Dennis SeiwertHannes WittAndreas JanshoffHarald PaulsenNature PortfolioarticleMedicineRScienceQENScientific Reports, Vol 7, Iss 1, Pp 1-10 (2017)
institution	DOAJ
collection	DOAJ
language	EN
topic	Medicine R Science Q
spellingShingle	Medicine R Science Q Dennis Seiwert Hannes Witt Andreas Janshoff Harald Paulsen The non-bilayer lipid MGDG stabilizes the major light-harvesting complex (LHCII) against unfolding
description	Abstract In the photosynthetic apparatus of plants a high proportion of LHCII protein is needed to integrate 50% non-bilayer lipid MGDG into the lamellar thylakoid membrane, but whether and how the stability of the protein is also affected is not known. Here we use single-molecule force spectroscopy to map the stability of LHCII against mechanical unfolding along the polypeptide chain as a function of oligomerization state and lipid composition. Comparing unfolding forces between monomeric and trimeric LHCII demonstrates that the stability does not increase significantly upon trimerization but can mainly be correlated with specific contact sites between adjacent monomers. In contrast, unfolding of trimeric complexes in membranes composed of different thylakoid lipids reveals that the non-bilayer lipid MGDG substantially increases the mechanical stability of LHCII in many segments of the protein compared to other lipids such as DGDG or POPG. We attribute these findings to steric matching of conically formed MGDG and the hourglass shape of trimeric LHCII, thereby extending the role of non-bilayer lipids to the structural stabilization of membrane proteins in addition to the modulation of their folding, conformation and function.
format	article
author	Dennis Seiwert Hannes Witt Andreas Janshoff Harald Paulsen
author_facet	Dennis Seiwert Hannes Witt Andreas Janshoff Harald Paulsen
author_sort	Dennis Seiwert
title	The non-bilayer lipid MGDG stabilizes the major light-harvesting complex (LHCII) against unfolding
title_short	The non-bilayer lipid MGDG stabilizes the major light-harvesting complex (LHCII) against unfolding
title_full	The non-bilayer lipid MGDG stabilizes the major light-harvesting complex (LHCII) against unfolding
title_fullStr	The non-bilayer lipid MGDG stabilizes the major light-harvesting complex (LHCII) against unfolding
title_full_unstemmed	The non-bilayer lipid MGDG stabilizes the major light-harvesting complex (LHCII) against unfolding
title_sort	non-bilayer lipid mgdg stabilizes the major light-harvesting complex (lhcii) against unfolding
publisher	Nature Portfolio
publishDate	2017
url	https://doaj.org/article/36d83c49dce9466c82514e87ffab3aed
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The non-bilayer lipid MGDG stabilizes the major light-harvesting complex (LHCII) against unfolding

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