Secretion of a bacterial cellulase by yeast.
Science
; 230(4728): 958-60, 1985 Nov 22.
Article
em En
| MEDLINE
| ID: mdl-17739223
ABSTRACT
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.
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Base de dados:
MEDLINE
Idioma:
En
Ano de publicação:
1985
Tipo de documento:
Article