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; Cristina Pagliano

doi:10.1038/s41467-020-15184-1

Nature Communications (Mar 2020)

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,
Cristina Pagliano

Affiliations

Pascal Albanese: Applied Science and Technology Department–BioSolar Lab, Politecnico di Torino
Sem Tamara: Biomolecular Mass Spectrometry and Proteomics, Bijvoet Center for Biomolecular Research and Utrecht Institute for Pharmaceutical Sciences, University of Utrecht
Guido Saracco: Applied Science and Technology Department–BioSolar Lab, Politecnico di Torino
Richard A. Scheltema: Biomolecular Mass Spectrometry and Proteomics, Bijvoet Center for Biomolecular Research and Utrecht Institute for Pharmaceutical Sciences, University of Utrecht
Cristina Pagliano: Applied Science and Technology Department–BioSolar Lab, Politecnico di Torino

DOI: https://doi.org/10.1038/s41467-020-15184-1
Journal volume & issue: Vol. 11, no. 1
pp. 1 – 14

Abstract

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The supramolecular organization of PSII-LHCII supercomplexes determines the plant thylakoid structure. Here, via structural mass spectrometry, Albanese et al. show how stroma-exposed N-termini of LHCII subunits, interacting with each other in adjacent membranes, can mediate membrane folding in grana stacks.

Published in Nature Communications

ISSN: 2041-1723 (Online)
Publisher: Nature Portfolio
Country of publisher: United Kingdom
LCC subjects: Science
Website: https://www.nature.com/ncomms/

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