1. Conformational dynamics of light-harvesting complex II in a native membrane environment
- Author
-
Azadi-Chegeni, Fatemeh, Ward, Meaghan E., Perin, Giorgio, Simionato, Diana, Morosinotto, Tomas, Baldus, Marc, Pandit, Anjali, Sub NMR Spectroscopy, NMR Spectroscopy, Sub NMR Spectroscopy, and NMR Spectroscopy
- Subjects
Chlorophyll ,In situ ,Light-Harvesting Protein Complexes ,Biophysics ,Chlamydomonas reinhardtii ,010402 general chemistry ,Photosynthesis ,Thylakoids ,01 natural sciences ,03 medical and health sciences ,chemistry.chemical_compound ,0302 clinical medicine ,Organelle ,Lipid bilayer ,030304 developmental biology ,0303 health sciences ,biology ,Chemistry ,Photosystem II Protein Complex ,food and beverages ,Articles ,Nuclear magnetic resonance spectroscopy ,biology.organism_classification ,0104 chemical sciences ,Membrane ,Thylakoid ,Helix ,030217 neurology & neurosurgery ,Violaxanthin - Abstract
Photosynthetic light-harvesting complexes of higher plants, moss and green algae can undergo dynamic conformational transitions, which have been correlated to their ability to adapt to fluctuations in the light environment. Herein, we demonstrate the application of solid-state NMR spectroscopy on native, heterogeneous thylakoid membranes of Chlamydomonas reinhardtii (Cr) and on Cr Light-Harvesting Complex II (LHCII) in thylakoid lipid bilayers to detect LHCII conformational dynamics in its native membrane environment. We show that membrane-reconstituted LHCII contains selective sites that undergo fast, large-amplitude motions, including the phytol tails of two chlorophylls. Protein plasticity is also observed in the N-terminal stromal loop and in protein fragments facing the lumen, involving sites that stabilize the xanthophyll-cycle carotenoid violaxanthin and the two luteins. The results report on the intrinsic flexibility of LHCII pigment-protein complexes in a membrane environment, revealing putative sites for conformational switching. In thylakoid membranes, fast dynamics of protein and pigment sites is significantly reduced, which suggests that in their native organelle membranes, LHCII complexes are locked in specific conformational states.STATEMENT OF SIGNIFICANCEPhotosynthetic Light-Harvesting Complexes undergo dynamic conformational transitions that regulate the capacity of the light-harvesting antenna. We demonstrate the application of solid-state (ss)NMR spectroscopy to investigate the structural dynamics of LHCII, the most abundant LHC complex of plants and algae, in native membranes. Selective dynamic protein and pigment residues are identified that are putative sites for a conformational switch.
- Published
- 2021