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Science 22 November 1985:
Vol. 230. no. 4728, pp. 958 - 960
DOI: 10.1126/science.230.4728.958
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Articles

Secretion of a Bacterial Cellulase by Yeast

NIGEL SKIPPER 1, MARGARET SUTHERLAND 1, R. WAYNE DAVIES 1, DOUGLAS KILBURN 2, ROBERT C. MILLER JR. 2, ANTHONY WARREN 2, and RAYMOND WONG 2

1 Division of Molecular Biology, Allelix, Inc., Mississauga, Ontario, Canada L4V 1P1
2 Department of Microbiology, University of British Columbia, Vancouver, British Columbia, Canada V6T 1W5

Gene fusions were constructed between a yeast expression plasmid and a Cellulomonas fimi DNA fragment encoding an endo-1,4-beta-D-glucanase or carboxymethylcellulase. Yeast transformed with the recombinant plasmids secreted carboxymethylcellulase activity. Secretion of active enzyme was greatly increased when the leader of a secreted yeast protein, the Kl toxin, was inserted immediately upstream of and in frame with the bacterial cellulase sequence. This is the first step in constructing a functional cellulase complex in Saccharomyces cerevisiae. It also provides an excellent system for the detailed examination of the determinants of protein secretion because of the ease with which secreted cellulase can be detected.

Submitted on March 4, 1985
Accepted on July 31, 1985


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