Photosystem II Regulation and Dynamics of the Chloroplast D1 Protein in Arabidopsis Leaves during Photosynthesis and Photoinhibition
Author(s) -
A. Wendy Russell,
Christa Critchley,
Sharon A. Robinson,
Linda A. Franklin,
GGR. Seaton,
W. S. Chow,
Jan M. Anderson,
C. B. Osmond
Publication year - 1995
Publication title -
plant physiology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 3.554
H-Index - 312
eISSN - 1532-2548
pISSN - 0032-0889
DOI - 10.1104/pp.107.3.943
Subject(s) - antheraxanthin , photosystem ii , dcmu , photoinhibition , photoprotection , photosynthesis , xanthophyll , biology , chlorophyll fluorescence , violaxanthin , photochemistry , biophysics , chemistry , zeaxanthin , biochemistry , lutein , carotenoid
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 non-photochemical 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.
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