How paired PSII–LHCII supercomplexes mediate the stacking of plant thylakoid membranes unveiled by structural mass-spectrometry

Pascal Albanese, Sem Tamara, Guido Saracco, Richard A. Scheltema () and Cristina Pagliano ()
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Pascal Albanese: Politecnico di Torino
Sem Tamara: University of Utrecht
Guido Saracco: Politecnico di Torino
Richard A. Scheltema: University of Utrecht
Cristina Pagliano: Politecnico di Torino

Nature Communications, 2020, vol. 11, issue 1, 1-14

Abstract: Abstract Grana are a characteristic feature of higher plants’ thylakoid membranes, consisting of stacks of appressed membranes enriched in Photosystem II (PSII) and associated light-harvesting complex II (LHCII) proteins, together forming the PSII-LHCII supercomplex. Grana stacks undergo light-dependent structural changes, mainly by reorganizing the supramolecular structure of PSII-LHCII supercomplexes. LHCII is vital for grana formation, in which also PSII-LHCII supercomplexes are involved. By combining top-down and crosslinking mass spectrometry we uncover the spatial organization of paired PSII-LHCII supercomplexes within thylakoid membranes. The resulting model highlights a basic molecular mechanism whereby plants maintain grana stacking at changing light conditions. This mechanism relies on interactions between stroma-exposed N-terminal loops of LHCII trimers and Lhcb4 subunits facing each other in adjacent membranes. The combination of light-dependent LHCII N-terminal trimming and extensive N-terminal α-acetylation likely affects interactions between pairs of PSII-LHCII supercomplexes across the stromal gap, ultimately mediating membrane folding in grana stacks.

Date: 2020
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DOI: 10.1038/s41467-020-15184-1

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