REDOX REGULATION OF LIGHT-HARVESTING COMPLEX-II AND CAB MESSENGER-RNA ABUNDANCE IN DUNALIELLA-SALINA

We demonstrate that photosynthetic adjustment at the level of the light-harvesting complex associated with photosystem II (LCH II) in Dunaliella salina is a response to changes in the redox state of intersystem electron transport as estimated by photosystem II (PSII) excitation pressure. To elucidate the molecular basis of this phenomenon, LHCII apoprotein accumulation and cab mRNA abundance were examined. Growth regimes that induced low, but equivalent, excitation pressures (either 13 degrees C/20 mu mol m(-2) s(-1) or 30 degrees C/150 mu mol m(-2) s(-1)) resulted in increased LHCII apoprotein and cab mRNA accumulation relative to algal cultures grown under high excitation pressures (either 13 degrees C/150 mu mol m(-2) s(-1) or 30 degrees C/2500 mu mol m(-2) s(-1)). Thermodynamic relaxation of high excitation pressures, accomplished by shifting cultures from a 13 to a 30 degrees C growth regime at constant irradiance for 12 h, resulted in a 6- and 8-fold increase in LHCII apoprotein and cab mRNA abundance, respectively. Similarly, photodynamic relaxation of high excitation pressure, accomplished by a shift from a light to a dark growth regime at constant temperature, resulted in a 2.4- to 4-fold increase in LHCII apoprotein and cab mRNA levels, respectively. We conclude that photosynthetic adjustment to temperature mimics adjustment to high irradiance through a common redox sensing/signaling mechanism. Both temperature and light modulate the redox state of the first, stable quinone electron acceptor of PSII, which reflects the redox poise of intersystem electron transport. Changes in redox poise signal the nucleus to regulate cab mRNA abundance, which, in turn, determines the accumulation of light-harvesting apoprotein. This redox mechanism may represent a general acclimation mechanism for photosynthetic adjustment to environmental stimuli.