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Authors: Seiwert, Dennis
Witt, Hannes
Janshoff, Andreas
Paulsen, Harald
Title: The non-bilayer lipid MGDG stabilizes the major light-harvesting complex (LHCII) against unfolding
Online publication date: 19-Oct-2022
Year of first publication: 2017
Language: english
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.
DDC: 580 Pflanzen (Botanik)
580 Botanical sciences
Institution: Johannes Gutenberg-Universität Mainz
Department: FB 10 Biologie
Place: Mainz
Version: Published version
Publication type: Zeitschriftenaufsatz
License: CC BY
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Journal: Scientific reports
Pages or article number: Art. 5158
Publisher: Macmillan Publishers Limited, part of Springer Nature
Publisher place: London
Issue date: 2017
ISSN: 2045-2322
Publisher URL:
Publisher DOI: 10.1038/s41598-017-05328-7
Appears in collections:DFG-OA-Publizieren (2012 - 2017)

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