Pea PSII-LHCII supercomplexes form pairs by making connections across the stromal gap

Albanese, Pascal and Melero, Roberto and Engel, Benjamin D. and Grinzato, Alessandro and Berto, Paola and Manfredi, Marcello and Chiodoni, Angelica and Vargas, Javier and Sorzano, Carlos Óscar Sánchez and Marengo, Emilio and Saracco, Guido and Zanotti, Giuseppe and Carazo, Jose-Maria and Pagliano, Cristina. (2017) Pea PSII-LHCII supercomplexes form pairs by making connections across the stromal gap. Scientific Reports, 7 (1). p. 10067.

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In higher plant thylakoids, the heterogeneous distribution of photosynthetic protein complexes is a determinant for the formation of grana, stacks of membrane discs that are densely populated with Photosystem II (PSII) and its light harvesting complex (LHCII). PSII associates with LHCII to form the PSII-LHCII supercomplex, a crucial component for solar energy conversion. Here, we report a biochemical, structural and functional characterization of pairs of PSII-LHCII supercomplexes, which were isolated under physiologically-relevant cation concentrations. Using single-particle cryo-electron microscopy, we determined the three-dimensional structure of paired C; 2; S; 2; M PSII-LHCII supercomplexes at 14 Å resolution. The two supercomplexes interact on their stromal sides through a specific overlap between apposing LHCII trimers and via physical connections that span the stromal gap, one of which is likely formed by interactions between the N-terminal loops of two Lhcb4 monomeric LHCII subunits. Fast chlorophyll fluorescence induction analysis showed that paired PSII-LHCII supercomplexes are energetically coupled. Molecular dynamics simulations revealed that additional flexible physical connections may form between the apposing LHCII trimers of paired PSII-LHCII supercomplexes in appressed thylakoid membranes. Our findings provide new insights into how interactions between pairs of PSII-LHCII supercomplexes can link adjacent thylakoids to mediate the stacking of grana membranes.
Faculties and Departments:05 Faculty of Science > Departement Biozentrum > Structural Biology & Biophysics > Structural Biology and Biophysics (Engel)
UniBasel Contributors:Engel, Ben
Item Type:Article, refereed
Article Subtype:Research Article
Publisher:Nature Publishing Group
Note:Publication type according to Uni Basel Research Database: Journal article
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Last Modified:23 Aug 2022 10:49
Deposited On:23 Aug 2022 10:49

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