Scientific article
Open access

Identification of a photosystem II phosphatase involved in light acclimation in Arabidopsis

Published inThe Plant cell, vol. 24, no. 6, p. 2596-2609
Publication date2012

Reversible protein phosphorylation plays a major role in the acclimation of the photosynthetic apparatus to changes in light. Two paralogous kinases phosphorylate subsets of thylakoid membrane proteins. STATE TRANSITION7 (STN7) phosphorylates LHCII, the light-harvesting antenna of photosystem II (PSII), to balance the activity of the two photosystems through state transitions. STN8, which is mainly involved in phosphorylation of PSII core subunits, influences folding of the thylakoid membranes and repair of PSII after photodamage. The rapid reversibility of these acclimatory responses requires the action of protein phosphatases. In a reverse genetic screen, we identified the chloroplast PP2C phosphatase, PHOTOSYSTEM II CORE PHOSPHATASE (PBCP), which is required for efficient dephosphorylation of PSII proteins. Its targets, identified by immunoblotting and mass spectrometry, largely coincide with those of the kinase STN8. The recombinant phosphatase is active in vitro on a synthetic substrate or on isolated thylakoids. Thylakoid folding is affected in the absence of PBCP, while its overexpression alters the kinetics of state transitions. PBCP and STN8 form an antagonistic kinase and phosphatase pair whose substrate specificity and physiological functions are distinct from those of STN7 and the counteracting phosphatase PROTEIN PHOSPHATASE1/THYLAKOID-ASSOCIATED PHOSPHATASE38, but their activities may overlap to some degree.

Citation (ISO format)
SAMOL, Iga et al. Identification of a photosystem II phosphatase involved in light acclimation in Arabidopsis. In: The Plant cell, 2012, vol. 24, n° 6, p. 2596–2609. doi: 10.1105/tpc.112.095703
Main files (1)
Article (Accepted version)
ISSN of the journal1040-4651

Technical informations

Creation11/06/2012 2:52:00 PM
First validation11/06/2012 2:52:00 PM
Update time03/14/2023 5:44:15 PM
Status update03/14/2023 5:44:14 PM
Last indexation01/16/2024 12:28:15 AM
All rights reserved by Archive ouverte UNIGE and the University of GenevaunigeBlack