Aw. Russell et al., PHOTOSYSTEM-II REGULATION AND DYNAMICS OF THE CHLOROPLAST D1 PROTEIN IN ARABIDOPSIS LEAVES DURING PHOTOSYNTHESIS AND PHOTOINHIBITION, Plant physiology, 107(3), 1995, pp. 943-952
Arabidopsis thaliana leaves were examined in short-term (1 h) and long
-term (10 h) irradiance experiments involving growth, saturating and e
xcess light. Changes in photosynthetic and chlorophyll fluorescence pa
rameters and in populations of functional photosystem II (PSII) center
s were independently measured. Xanthophyll pigments, 3-(3,4-dichloroph
enyl)-1,1-dimethylurea (DCMU)-binding sites, the amounts of D1 protein
, and the rates of D1 protein synthesis were determined. These compreh
ensive studies revealed that under growth or light-saturating conditio
ns, photosynthetic parameters remained largely unaltered. Photoprotect
ion occurred at light saturation indicated by a dark-reversible increa
se in nonphotochemical quenching accompanied by a 5-fold increase in a
ntheraxanthin and zeaxanthin. No consistent change in the concentratio
ns of functional PSII centers, DCMU-binding sites, or D1 protein pool
size occurred. D1 protein synthesis was rapid. In excess irradiance, q
uantum yield of O-2 evolution and the efficiency of PSII were reduced,
associated with a 15- to 20-fold increase in antheraxanthin and zeaxa
nthin and a sustained increase in nonphotochemical quenching. A decrea
se in functional PSII center concentration occurred, followed by a dec
line in the concentration of D1 protein; the latter, however, was not
matched by a decrease in DCMU-binding sites. In the most extreme treat
ments, DCMU-binding site concentration remained 2 times greater than t
he concentration of D1 protein recognized by antibodies. D1 protein sy
nthesis rates remained unaltered at excess irradiances.