Wood, W.H.J., Barnett, S.F.H., Flannery, S. et al. (2 more authors) (2019) Dynamic thylakoid stacking is regulated by LHCII phosphorylation but not its interaction with PSI. Plant Physiology, 180 (4). pp. 2152-2166. ISSN 0032-0889
Abstract
Grana stacking in plant chloroplast thylakoid membranes dynamically responds to the light environment. These dynamics have been linked to regulation of the relative antenna sizes of PSI and PSII (state transitions), the PSII repair cycle, and the regulation of photosynthetic electron transfer. Here, we used 3D structured illumination microscopy, a subdiffraction-resolution fluorescence imaging technique, to investigate the light-intensity dependence, kinetics, reversibility, and regulation of dynamic thylakoid stacking in spinach (Spinacia oleracea) and Arabidopsis (Arabidopsis thaliana). Low-intensity white light (150 μmol photons m−2 s−1) behaved similarly to light preferentially exciting PSII (660 nm), causing a reduction in grana diameter and an increased number of grana per chloroplast. By contrast, high-intensity white light (1000 μmol photons m−2 s−1), darkness, and light preferentially exciting PSI (730 nm) reversed these changes. These dynamics occurred with a half-time of 7 to 8 min and were accompanied by state transitions. Consistent with this, the dynamics were dependent on STN7 (light-harvesting complex II [LHCII] kinase) and TAP38 (LHCII phosphatase), which are required for state transitions but were unaffected by the absence of STN8 (PSII kinase) or PSII core phosphatase (PSII phosphatase). Unlike state transitions, however, thylakoid stacking dynamics did not rely on the presence of the LHCI and PSI subunit L phospho-LHCII binding sites on PSI. Since oligomerization of thylakoid curvature protein (CURT1A) was unaffected by the absence of STN7 or TAP38, we conclude that the primary determinant of dynamic thylakoid stacking is LHCII phosphorylation.
Metadata
Item Type: | Article |
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Authors/Creators: |
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Copyright, Publisher and Additional Information: | © 2019 American Society of Plant Biologists. This is an author-produced version of a paper subsequently published in Plant Physiology. Uploaded in accordance with the publisher's self-archiving policy. |
Dates: |
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Institution: | The University of Sheffield |
Academic Units: | The University of Sheffield > Faculty of Science (Sheffield) > School of Biosciences (Sheffield) > Department of Molecular Biology and Biotechnology (Sheffield) |
Funding Information: | Funder Grant number Leverhulme Trust (The) RPG-2016-161; RPG-2019-045 Biotechnology and Biological Sciences Research Council (BBSRC) BB/P002005/1 |
Depositing User: | Symplectic Sheffield |
Date Deposited: | 25 Sep 2019 13:32 |
Last Modified: | 25 Sep 2019 13:32 |
Status: | Published |
Publisher: | American Society of Plant Biologists (ASPB) |
Refereed: | Yes |
Identification Number: | 10.1104/pp.19.00503 |
Related URLs: | |
Open Archives Initiative ID (OAI ID): | oai:eprints.whiterose.ac.uk:151343 |