The expression of actin genes was examined during oogenesis of Drosophila. Accumulation of actin proteins was quantitated by a two-stage electrophoresis procedure. Egg chambers accumulate actins preferentially, resulting in a twofold enrichment over other nonyolk proteins. RNA gel blot hybridization experiments demonstrated a concomitant twofold selective increase of actin mRNA levels over that of other mRNAs, suggesting regulation of actin genes at the pretranslational level. Despite an abrupt arrest of actin protein accumulation near the end of oogenesis, the bulk of the actin mRNAs remains associated with polysomes of constant size. It appears that this shut-off of actin protein accumulation is due to an overall decrease in translational efficiency, rather than actin mRNA degradation or its dissociation from polysomes.
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