Regulation of excitation energy in a wheat mutant deficient in light-harvesting pigment protein complex.

Chloroplasts of the CD3 wheat mutant were deficient primarily in chlorophyll of light harvesting pigment proteins (LHPP) 1 and 2 and CP1a. The reduced level of protein associated with chlorophyll of LHPP1 and LHPP2 and the reduced level of low molecular weight polypeptides between 23 and 29 kilodaltons confirmed that the CD3 mutant was deficient in the LHPP complex. The high fluorescence emission ratio at 740 (F740) to 686 nanometers (F686) observed from chloroplasts of normal wheat following light induced phosphorylation of the LHPP complex was not noted from mutant chloroplasts. The long wavelength peak fluorescence emission (F740) was shifted to a shorter wavelength peak (F725) and was reduced in intensity compared to that of normal wheat thylakoids. The ratio of variable fluorescence to maximum fluorescence, a measure of PSII photochemical efficiency, was the same for the normal wheat and mutant leaves. The ratios of uncoupled photosystem I/photosystem II electron transport rates for mutant and normal wheat chloroplasts were similar at saturating light suggesting that absorbed excitation energy was distributed to the two photosystem reaction centers of the mutant in a similar manner as in the normal wheat. Proteins of the LHPP complex were differentially phosphorylated by action of a membrane protein kinase when both normal wheat and CD3 mutant thylakoids were irradiated without an electron transport chain acceptor. Even though the F740/F686 ratio was low in mutant thylakoids, the phosphorylation of the 27-kilodalton LHPP polypeptide was consistent with the mutant being in a state II condition. The data gave rise to the suggestion that the F740/F686 ratio might not indicate excitation energy distribution to the two photosystems in the mutant.