Issue 5, 2020

Composition, phosphorylation and dynamic organization of photosynthetic protein complexes in plant thylakoid membrane

Abstract

The photosystems (PS), catalyzing the photosynthetic reactions of higher plants, are unevenly distributed in the thylakoid membrane: PSII, together with its light harvesting complex (LHC)II, is enriched in the appressed grana stacks, while PSI–LHCI resides in the non-appressed stroma thylakoids, which wind around the grana stacks. The two photosystems interact in a third membrane domain, the grana margins, which connect the grana and stroma thylakoids and allow the loosely bound LHCII to serve as an additional antenna for PSI. The light harvesting is balanced by reversible phosphorylation of LHCII proteins. Nevertheless, light energy also damages PSII and the repair process is regulated by reversible phosphorylation of PSII core proteins. Here, we discuss the detailed composition and organization of PSII–LHCII and PSI–LHCI (super)complexes in the thylakoid membrane of angiosperm chloroplasts and address the role of thylakoid protein phosphorylation in dynamics of the entire protein complex network of the photosynthetic membrane. Finally, we scrutinize the phosphorylation-dependent dynamics of the protein complexes in context of thylakoid ultrastructure and present a model on the reorganization of the entire thylakoid network in response to changes in thylakoid protein phosphorylation.

Graphical abstract: Composition, phosphorylation and dynamic organization of photosynthetic protein complexes in plant thylakoid membrane

Article information

Article type
Perspective
Submitted
30 1 2020
Accepted
27 3 2020
First published
16 4 2020
This article is Open Access
Creative Commons BY license

Photochem. Photobiol. Sci., 2020,19, 604-619

Composition, phosphorylation and dynamic organization of photosynthetic protein complexes in plant thylakoid membrane

M. Rantala, S. Rantala and E. Aro, Photochem. Photobiol. Sci., 2020, 19, 604 DOI: 10.1039/D0PP00025F

This article is licensed under a Creative Commons Attribution 3.0 Unported Licence. You can use material from this article in other publications without requesting further permissions from the RSC, provided that the correct acknowledgement is given.

Read more about how to correctly acknowledge RSC content.

Spotlight

Advertisements