Photosystem II Regulation and Dynamics of the Chloroplast D1 Protein in Arabidopsis Leaves during Photosynthesis and Photoinhibition

• Published in: Plant physiology (Bethesda) Vol. 107; no. 3; pp. 943 - 952
• Main Authors: A. Wendy Russell, Critchley, Christa, Sharon A. Robinson, Linda A. Franklin, George G. R. Seaton, Chow, Wah Soon, Anderson, Jan M., C. Barry Osmond
• Format: Journal Article
• Language: English
• Published: Rockville, MD American Society of Plant Physiologists 01.03.1995
• Subjects: Biological and medical sciences; Chlorophylls; Fluorescence; Fundamental and applied biological sciences. Psychology; Irradiance; Leaves; Metabolism; Photoinhibition; Photons; Photosynthesis; Photosynthesis, respiration. Anabolism, catabolism; Photosystem II; Plant physiology and development; Plants; Whole Plant, Environmental, and Stress Physiology; Xanthophylls; Short term; Plant leaf; Long term; Arabidopsis thaliana; Luminous intensity; Photosystem 2; Cruciferae; Photosynthetic pigment; Dicotyledones; Angiospermae; Photoinhibition; Spermatophyta; Experimental plant; Photosynthesis
• ISSN: 0032-0889; 1532-2548
• DOI: 10.1104/pp.107.3.943

Arabidopsis thaliana leaves were examined in short-term (1 h) and long-term (10 h) irradiance experiments involving growth, saturating and excess light. Changes in photosynthetic and chlorophyll fluorescence parameters and in populations of functional photosystem II (PSII) centers were independently measured. Xanthophyll pigments, 3-(3,4-dichlorophenyl)-1,1-dimethylurea (DCMU)-binding sites, the amounts of D1 protein, and the rates of D1 protein synthesis were determined. These comprehensive studies revealed that under growth or light-saturating conditions, photosynthetic parameters remained largely unaltered. Photoprotection occurred at light saturation indicated by a dark-reversible increase in nonphotochemical quenching accompanied by a 5-fold increase in antheraxanthin and zeaxanthin. No consistent change in the concentrations of functional PSII centers, DCMU-binding sites, or D1 protein pool size occurred. D1 protein synthesis was rapid. In excess irradiance, quantum yield of O2 evolution and the efficiency of PSII were reduced, associated with a 15- to 20-fold increase in antheraxanthin and zeaxanthin and a sustained increase in nonphotochemical quenching. A decrease in functional PSII center concentration occurred, followed by a decline in the concentration of D1 protein; the latter, however, was not matched by a decrease in DCMU-binding sites. In the most extreme treatments, DCMU-binding site concentration remained 2 times greater than the concentration of D1 protein recognized by antibodies. D1 protein synthesis rates remained unaltered at excess irradiances.