The A and B forms of the chicken progesterone receptor arise by alternate initiation of translation of a unique mRNA.

In order to establish the origin of the A and B proteins of the chicken progesterone receptor we have expressed its cDNA in vivo in heterologous cells and in vitro in reticulocyte cell lysates. The A and B proteins were expressed from a single cDNA both in heterologous receptor negative cells and in a cell-free system. Both proteins bind progesterone and are indistinguishable from chick oviduct authentic A and B proteins in terms of size, immunoreactivity and hormone binding properties. Truncated mRNA's which lack the receptor B protein translation signal are capable of generating the receptor A protein by initiation of translation at a second internal start site. We conclude from these data that the chicken progesterone receptor A and B proteins arise most likely by alternate initiation of translation from a single mRNA transcript.