Please use this identifier to cite or link to this item: http://doi.org/10.25358/openscience-8098
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dc.contributor.authorSeiwert, Dennis-
dc.contributor.authorWitt, Hannes-
dc.contributor.authorJanshoff, Andreas-
dc.contributor.authorPaulsen, Harald-
dc.date.accessioned2022-10-19T08:21:57Z-
dc.date.available2022-10-19T08:21:57Z-
dc.date.issued2017
dc.identifier.urihttps://openscience.ub.uni-mainz.de/handle/20.500.12030/8113-
dc.description.abstractIn 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.sponsorshipDFG, Open Access-Publizieren Universität Mainz / Universitätsmedizinde
dc.language.isoengde
dc.rightsCC BY*
dc.rights.urihttps://creativecommons.org/licenses/by/4.0/*
dc.subject.ddc580 Pflanzen (Botanik)de_DE
dc.subject.ddc580 Botanical sciencesen_GB
dc.titleThe non-bilayer lipid MGDG stabilizes the major light-harvesting complex (LHCII) against unfoldingen_GB
dc.typeZeitschriftenaufsatzde
dc.identifier.doihttp://doi.org/10.25358/openscience-8098-
jgu.type.dinitypearticleen_GB
jgu.type.versionPublished versionde
jgu.type.resourceTextde
jgu.organisation.departmentFB 10 Biologiede
jgu.organisation.number7970-
jgu.organisation.nameJohannes Gutenberg-Universität Mainz-
jgu.rights.accessrightsopenAccess-
jgu.journal.titleScientific reportsde
jgu.journal.volume7de
jgu.journal.issue1de
jgu.pages.alternativeArt. 5158de
jgu.publisher.year2017-
jgu.publisher.nameMacmillan Publishers Limited, part of Springer Naturede
jgu.publisher.placeLondonde
jgu.publisher.urihttp://dx.doi.org/10.1038/s41598-017-05328-7de
jgu.publisher.issn2045-2322de
jgu.organisation.placeMainz-
jgu.subject.ddccode580de
opus.date.modified2018-04-03T07:15:28Z
opus.subject.dfgcode00-000
opus.organisation.stringFB 10: Biologie: Institut für Molekulare Physiologiede_DE
opus.identifier.opusid57071
opus.institute.number1013
opus.metadataonlyfalse
opus.type.contenttypeKeinede_DE
opus.type.contenttypeNoneen_EN
opus.affiliatedPaulsen, Harald
jgu.publisher.doi10.1038/s41598-017-05328-7de
jgu.organisation.rorhttps://ror.org/023b0x485-
Appears in collections:DFG-OA-Publizieren (2012 - 2017)

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