Abstract

The levels of peridinin-chlorophyll a -protein (PCP) mRNA, apoprotein and protein bound with peridinin (holoprotein) were measured as a function of circadian time in the dinoflagellate Gonyaulax polyedra to test involvement of this protein in the circadian oxygen evolution rhythm. This involvement was suggested by previous work showing that synthesis of PCP was rhythmic in vivo and in phase with the three-fold rhythm of oxygen evolution. However, Gonyaulax contains six PCP isoforms, only one of which was previously examined. In this report, we extend our analysis to two additional isoforms to encompass roughly 90% of the total cellular PCP. We confirm that synthesis of two additional PCP isoforms is rhythmic in vivo and show that this regulation appears to occur at a translational level as found for two other regulated proteins in this organism. However, PCP is unlikely to be implicated in the oxygen evolution rhythm since both PCP protein levels and the amount of chromophore (OD480) bound to protein (OD280) are constant over a circadian period.

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