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

Albanese, P., Melero, R., Engel, B. D., Grinzato, A., Berto, P., Manfredi, M., et al. (2017). Pea PSII-LHCII supercomplexes form pairs by making connections across the stromal gap. Scientific Reports, 7: 10067. doi:10.1038/s41598-017-10700-8.

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 Creators:
Albanese, Pascal1, Author
Melero, Roberto1, Author
Engel, Benjamin D.2, Author           
Grinzato, Alessandro1, Author
Berto, Paola1, Author
Manfredi, Marcello1, Author
Chiodoni, Angelica1, Author
Vargas, Javier1, Author
Sanchez Sorzano, Carlos Oscar1, Author
Marengo, Emilio1, Author
Saracco, Guido1, Author
Zanotti, Giuseppe1, Author
Carazo, Jose-Maria1, Author
Pagliano, Cristina1, Author
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1external, ou_persistent22              
2Baumeister, Wolfgang / Molecular Structural Biology, Max Planck Institute of Biochemistry, Max Planck Society, ou_1565142              

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Free keywords: LIGHT-HARVESTING COMPLEX; PHOTOSYSTEM-II SUPERCOMPLEXES; EM STRUCTURE DETERMINATION; MOLECULAR-DYNAMICS METHOD; THYLAKOID MEMBRANES; ELECTRON-MICROSCOPY; SUPRAMOLECULAR ORGANIZATION; GRANA STACKING; GREEN PLANTS; PHOTOSYNTHETIC MEMBRANEScience & Technology - Other Topics;
 Abstract: 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 C2S2M PSII-LHCII supercomplexes at 14 angstrom 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.

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Language(s): eng - English
 Dates: 2017
 Publication Status: Published online
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Title: Scientific Reports
  Abbreviation : Sci. Rep.
Source Genre: Journal
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Publ. Info: London, UK : Nature Publishing Group
Pages: - Volume / Issue: 7 Sequence Number: 10067 Start / End Page: - Identifier: ISSN: 2045-2322
CoNE: https://pure.mpg.de/cone/journals/resource/2045-2322