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

Please use this identifier to cite or link to this item: http://doi.org/10.25358/openscience-8098

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DC Field	Value	Language
dc.contributor.author	Seiwert, Dennis	-
dc.contributor.author	Witt, Hannes	-
dc.contributor.author	Janshoff, Andreas	-
dc.contributor.author	Paulsen, Harald	-
dc.date.accessioned	2022-10-19T08:21:57Z	-
dc.date.available	2022-10-19T08:21:57Z	-
dc.date.issued	2017
dc.identifier.uri	https://openscience.ub.uni-mainz.de/handle/20.500.12030/8113	-
dc.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.	en_GB
dc.description.sponsorship	DFG, Open Access-Publizieren Universität Mainz / Universitätsmedizin	de
dc.language.iso	eng	de
dc.rights	CC BY	*
dc.rights.uri	https://creativecommons.org/licenses/by/4.0/	*
dc.subject.ddc	580 Pflanzen (Botanik)	de_DE
dc.subject.ddc	580 Botanical sciences	en_GB
dc.title	The non-bilayer lipid MGDG stabilizes the major light-harvesting complex (LHCII) against unfolding	en_GB
dc.type	Zeitschriftenaufsatz	de
dc.identifier.doi	http://doi.org/10.25358/openscience-8098	-
jgu.type.dinitype	article	en_GB
jgu.type.version	Published version	de
jgu.type.resource	Text	de
jgu.organisation.department	FB 10 Biologie	de
jgu.organisation.number	7970	-
jgu.organisation.name	Johannes Gutenberg-Universität Mainz	-
jgu.rights.accessrights	openAccess	-
jgu.journal.title	Scientific reports	de
jgu.journal.volume	7	de
jgu.journal.issue	1	de
jgu.pages.alternative	Art. 5158	de
jgu.publisher.year	2017	-
jgu.publisher.name	Macmillan Publishers Limited, part of Springer Nature	de
jgu.publisher.place	London	de
jgu.publisher.uri	http://dx.doi.org/10.1038/s41598-017-05328-7	de
jgu.publisher.issn	2045-2322	de
jgu.organisation.place	Mainz	-
jgu.subject.ddccode	580	de
opus.date.modified	2018-04-03T07:15:28Z
opus.subject.dfgcode	00-000
opus.organisation.string	FB 10: Biologie: Institut für Molekulare Physiologie	de_DE
opus.identifier.opusid	57071
opus.institute.number	1013
opus.metadataonly	false
opus.type.contenttype	Keine	de_DE
opus.type.contenttype	None	en_EN
opus.affiliated	Paulsen, Harald
jgu.publisher.doi	10.1038/s41598-017-05328-7	de
jgu.organisation.ror	https://ror.org/023b0x485	-
Appears in collections:	DFG-OA-Publizieren (2012 - 2017)

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