Regulation of a Bifunctional mRNA Results in Synthesis of Secreted and Nuclear Probasin

• Published in: Proceedings of the National Academy of Sciences - PNAS 1989-10, Vol.86 (20), p.7843-7847
• Main Authors: Spence, Andrew M., Sheppard, Patricia C., Davie, James R., Matuo, Yuhsi, Nishi, Nozomu, McKeehan, Wallace L., Dodd, Janice G., Matusik, Robert J.
• Format: Article
• Language: English
• Subjects: Amino Acid Sequence; Amino acids; Androgen-Binding Protein - biosynthesis; Androgen-Binding Protein - genetics; Androgen-Binding Protein - metabolism; Animals; Base Sequence; Cell Nucleus - metabolism; Cloning, Molecular; Codon - genetics; Codons; Complementary DNA; Epithelial cells; Genes; Genes, Regulator; Immunoenzyme Techniques; Male; Messenger RNA; Molecular Sequence Data; Nuclear proteins; Nucleotides; Prostate; Prostate - metabolism; Protein Biosynthesis; Proteins; Rats; RNA, Messenger - genetics; Secretion; Sequence Homology, Nucleic Acid
• ISSN: 0027-8424; 1091-6490
• DOI: 10.1073/pnas.86.20.7843

Probasin, a rat prostatic protein, is statistically related to members of a protein family that includes serum, cellular, and nuclear proteins. In vivo, probasin appears both in the secretions and in the nucleus of prostatic epithelial cells. Using primer extension and S1 nuclease protection assays we detected only one probasin mRNA. Thus, the localization of this protein to two separate cellular regions must be encoded by this one mRNA. Furthermore, in vitro translation of synthetic probasin mRNA demonstrated that a protein containing a signal peptide and a protein lacking a signal peptide were synthesized by initiation at different AUG codons. These data are consistent with a mechanism of translational regulation of a eukaryotic bifunctional mRNA.