Why we need to know the structure of phosphorylated chloroplast light‐harvesting complex II

• Published in: Physiologia plantarum Vol. 161; no. 1; pp. 28 - 44
• Main Author: Allen, John F.
• Format: Journal Article
• Language: English
• Published: Oxford, UK Blackwell Publishing Ltd 01.09.2017; Wiley Subscription Services, Inc
• Subjects: Adaptations; Binding sites; Chlorophyll; Chloroplast Proteins - metabolism; Chloroplasts; Chloroplasts - metabolism; Energy; Excitation; Light; Light-harvesting complex; Light-Harvesting Protein Complexes - chemistry; Light-Harvesting Protein Complexes - metabolism; N-Terminus; Phosphoproteins - metabolism; Phosphorylation; Photosynthesis; Photosynthetic apparatus; Photosystem I; Photosystem II; Photosystem II Protein Complex - metabolism; Protein structure; Quaternary structure; Secondary structure; Spectral composition; Steric effects
• ISSN: 0031-9317; 1399-3054
• DOI: 10.1111/ppl.12577

In oxygenic photosynthesis there are two ‘light states’ – adaptations of the photosynthetic apparatus to spectral composition that otherwise favours either photosystem I or photosystem II. In chloroplasts of green plants the transition to light state 2 depends on phosphorylation of apoproteins of a membrane‐intrinsic antenna, the chlorophyll‐a/b‐binding, light‐harvesting complex II (LHC II), and on the resulting redistribution of absorbed excitation energy from photosystem II to photosystem I. The transition to light state 1 reverses these events and requires a phospho‐LHC II phosphatase. Current structures of LHC II reveal little about possible steric effects of phosphorylation. The surface‐exposed N‐terminal domain of an LHC II polypeptide contains its phosphorylation site and is disordered in its unphosphorylated form. A molecular recognition hypothesis proposes that state transitions are a consequence of movement of LHC II between binding sites on photosystems I and II. In state 1, LHC II forms part of the antenna of photosystem II. In state 2, a unique but as yet unidentified 3‐D structure of phospho‐LHC II may attach it instead to photosystem I. One possibility is that the LHC II N‐terminus becomes ordered upon phosphorylation, adopting a local alpha‐helical secondary structure that initiates changes in LHC II tertiary and quaternary structure that sever contact with photosystem II while securing contact with photosystem I. In order to understand redistribution of absorbed excitation energy in photosynthesis we need to know the structure of LHC II in its phosphorylated form, and in its complex with photosystem I.