CLONING AND EXPRESSION OF HORMOCONIS-RESINAE GLUCOAMYLASE-P CDNA IN SACCHAROMYCES-CEREVISIAE

A cDNA coding for glucoamylase P of Hormoconis resinae was cloned usin g a synthetic oligonucleotide probe coding for a peptide fragment of t he purified enzyme and polyclonal anti-glucoamylase antibodies. Nucleo tide-sequence analysis revealed an open reading frame of 1848 base pai rs coding for a protein of 616 amino-acid residues. Comparison with ot her fungal glucoamylase amino-acid sequences showed homologies of 37-4 8%. The glucoamylase cDNA, when introduced into Saccharomyces cerevisi ae under the control of the yeast ADC1 promoter, directed the secretio n of active glucoamylase P into the growth medium.