In vitro synthesis of repressible yeast acid phosphatase: identification of multiple mRNAs and products.

Abstract

Antibodies to repressible nonspecific acid phosphatase [APase; orthophosphoric-monoester phosphohydrolase (acid optimum), EC 3.1.3.2] purified from S. cerevisiae were used to detect the in vitro products of APase mRNA. Immunoprecipitation of cell-free synthesized protein and of in vivo enzyme from cell extracts showed that derepression of enzyme synthesis in situ is the result of de novo appearance of functional mRNA followed by de novo protein synthesis. At least 3 unique APase polypeptides are synthesized in vitro from separate mRNA and appear to be glycosylated in vivo to form secreted enzyme.