By the use of glucoamylase-specific synthetic oligodeoxyribonucleotides and molecular cloning of cDNA synthesized from Aspergillus niger total poly(A) + RNA, the primary structure of the glucoamylase G1 mRNA was determined. Glucoamylase G1 is synthesized as a precursor of 640 amino acid residues containing a putative signal peptide of 18 residues, a short propeptide of six residues and the 616 residues long mature enzyme. In vitro translations of mRNA and immunoprecipitations with glucoamylase-specific antisera showed that two glucoamylase polypeptides are synthesized. The larger form with an apparent mol. wt. of 71 000 corresponds to the precursor of glucoamylase G1, and the shorter form with an apparent mol. wt. of 61 000 corresponds to the precursor of glucoamylase G2. From the nucleotide sequencing data of several glucoamylase-specific cDNA recombinants it is shown that the G1 mRNA contains a 169 bp long intervening sequence that can be spliced out to generate a G2 mRNA. Only the 3' part of the G1 mRNA is modified by this splicing event. This kind of differential mRNA processing to give different protein products from one primary transcript has previously only been demonstrated in higher eukaryotes.
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