Phased protein synthesis at several circadian times does not change protein levels in Gonyaulax.

The synthesis rates of 13 individual proteins in Gonyaulax polyedra, resolved by two-dimensional gel electrophoresis, were estimated from the amount of 35S methionine incorporated during in vivo pulse labeling at 2-h intervals over one circadian period. The synthesis rates of three proteins, taken as controls, varied 2-3 fold, and no systematic pattern to these variations was apparent. In contrast, the synthesis rates of 10 other proteins varied at least tenfold and in a smooth and systematic pattern. The patterns of protein synthesis were placed into three different groups, the first occurring during the late day/early night phase, the second during the middle of the night phase, and the third during the late night/early day phase. The length of time that individual proteins within each group could incorporate radiolabel was variable, raising the possibility that additional groups might be present. However, both a replicate experiment in continuous light and a light:dark experiment confirmed the presence of at least three different groups of protein synthesis patterns. Unlike the circadian changes in the synthesis rate of the luciferin binding protein, which produces variations in protein levels that correlate with the bioluminescence rhythm, no substantial changes were found in the levels of any other rhythmically synthesized proteins examined.