In vitro synthesis of repressible yeast acid phosphatase: identification of multiple mRNAs and products.
Antibodies to repressible nonspecific acid phosphatase [APase; orthophosphoric-monoester phosphohydrolase (acid optimum), EC 3.1.3.2] purified from Saccharomyces 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 has shown 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 three unique APase polypeptides are synthesized in vitro from separate mRNAs and appear to be glycosylated in vivo to form secreted enzyme.
D000135:Acid Phosphatase / Q000096:biosynthesis* / Q000235:genetics; D004794:Enzyme Repression / Q000187:drug effects; D005786:Gene Expression Regulation / Q000187:drug effects; D006023:Glycoproteins / Q000378:metabolism; D009154:Mutation; D010446:Peptide Fragments / Q000032:analysis; D010710:Phosphates / Q000494:pharmacology; D014176:Protein Biosynthesis; D012333:RNA, Messenger / Q000378:metabolism*; D012441:Saccharomyces cerevisiae / Q000378:metabolism
D006023:Glycoproteins; D010446:Peptide Fragments; D010710:Phosphates; D012333:RNA, Messenger; D000135:Acid Phosphatase