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Personen: Seiwert, Dennis (Autor) 
Witt, Hannes (Autor) 
Janshoff, Andreas (Autor) 
Paulsen, Harald (Autor) 
  
Titel: The non-bilayer lipid MGDG stabilizes the major light-harvesting complex (LHCII) against unfolding
  
Quelle: Scientific reports. Bd. 7. H. 1. London : Macmillan Publishers Limited, part of Springer Nature. Art. 5158
Erscheinungsjahr:    2017
ISBN / ISSN: 2045-2322
URL der Originalveröffentlichung doi:10.1038/s41598-017-05328-7
  
Dokumentart:
Zeitschriftenaufsatz Zeitschriftenaufsatz
Sprache: Englisch
Open Access: OpenAccess
Person der Universität:    Paulsen, Harald  In UnivIS suchen 
Einrichtung: Institut für Molekulare Physiologie
DDC-Sachgruppe:    Pflanzen (Botanik)
ID: 57071  Universitätsbibliothek Mainz
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Informationen zu den Nutzungsrechten unserer Inhalte Informationen zu den Nutzungsrechten unserer Inhalte
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.
   
  
Verfügbarkeit prüfen:    Rechercheportal Mainz: 2045-2322
  Elektronische Zeitschriftenbibliothek (EZB): 2045-2322
 


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