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Cloning and Expression of Hormoconis Resinae Glucoamylase P CDNA in Saccharomyces Cerevisiae

Overview
Journal Curr Genet
Specialty Genetics
Date 1993 Jul 1
PMID 8358830
Citations 4
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Abstract

A cDNA coding for glucoamylase P of Hormoconis resinae was cloned using a synthetic oligonucleotide probe coding for a peptide fragment of the purified enzyme and polyclonal anti-glucoamylase antibodies. Nucleotide-sequence analysis revealed an open reading frame of 1848 base pairs coding for a protein of 616 amino-acid residues. Comparison with other fungal glucoamylase amino-acid sequences showed homologies of 37-48%. The glucoamylase cDNA, when introduced into Saccharomyces cerevisiae under the control of the yeast ADC1 promoter, directed the secretion of active glucoamylase P into the growth medium.

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