Specific processing of the bacterial β‐lactamase precursor in Saccharomyces cerevisiae

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Abstract
Synthesis and processing of the bacterial enzyme β‐lactamase (E.C. 3.5. 2.6) were studied in Saccharomyces cerevisiae. The 2‐μm DNA vector pADH040‐2 containing the yeast ADH1 promoter fused to the bacterial gene was used in order to obtain enhanced synthesis of the bacterial protein in yeast transformants. Both precursor and mature β‐lactamase were shown to be present in yeast cells, the precursor being the major product. The mature enzyme was purified about 500‐fold over crude extracts to apparent homogeneity and thus represents nearly 0.2% of the total yeast protein. No difference in specific activity and molecular weight could be observed when compared with the authentic β‐lactamase from Escherichia coli. Specificity of the processing of β‐lactamase in yeast cells was verified by partial amino acid sequence analysis demonstrating the removal of the signal peptide at the correct position.

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