Regulation of translation of ovalbumin messenger RNA by estrogens and progesterone in oviduct of withdrawn chicks.

In the oviduct of chicks withdrawn from previous treatment with estrogens, no ovalbumin synthesis can be detected, although there are a limited number of ovalbumin mRNA sequences. These sequences are predominately associated with membrane-bound ribosomes. However, the size of the polysomes is small compared to those from the laying hen, suggesting that the inability to detect ovalbumin synthesis is the result of inefficient initiation of ovalbumin synthesis. When the rate of peptide chain elongation is reduced by treatment of chicks with cycloheximide, there is an increase in the average size of polysomes and a shift of ovalbumin mRNA sequences from small to large-sized polysomes. Readministration of estrogen to withdrawn chicks results in a time-dependent shift of monosomes to polysomes and a proportional shift of ovalbumin mRNA sequences between the two fractions, indicating that estrogen stimulates the rate of initiation of all mRNA species in the oviduct to essentially the same extent. In contrast, progesterone administration results in a preferential shift of ovalbumin mRNA relative to total RNA, suggesting a preferential effect of progesterone on initiation of protein synthesis with ovalbumin mRNA.