Genetic approach to secretion and hyperproduction of cellulases by Trichoderma. Progress report, August 1985-April 1986
The multienzyme cellulase complex of the mesophilic fungus Trichoderma reesei has been studied. Our laboratory has focused on the production of high yielding mutants and the analysis of these mutants with respect to the events involved in secretion of the enzymes. The effect of glycosylation inhibitors, tunicamycin and 2-deoxyglucose and membrane perturbing agents (ethanol and phenylethanol) have been studied at both the biochemical and morphological levels. Antibodies conjugated to gold-protein A particles have localized cellobiohydrolase in the endoplasmic reticulum, Golgi and secretory vesicle regions, confirming that this general pathway, which has been firmly identified in yeast and mammalian cells, also exists in Trichoderma. Temperature sensitive secretion mutants have been isolated and one mutant, LU-ts 1, was shown to be ts for cellulase and not for protease, amylase and xylanase. At the non-permissive temperature heterogeneous protein bands are exhibited by this mutant which are inactive. This characteristic of ts for secretion is reversible. At the permissive temperature normal cellulase enzymes are secreted. 2 refs.
- Research Organization:
- Lehigh Univ., Bethlehem, PA (USA)
- DOE Contract Number:
- AC02-83ER13106
- OSTI ID:
- 5878455
- Report Number(s):
- DOE/ER/13106-1; ON: DE86007858
- Country of Publication:
- United States
- Language:
- English
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59 BASIC BIOLOGICAL SCIENCES
BIOLOGICAL VARIABILITY
BIOSYNTHESIS
CELLULASE
DNA
ENZYMES
FUNGI
GENE MUTATIONS
GLYCOSYL HYDROLASES
HYDROLASES
MUTATIONS
NUCLEIC ACIDS
O-GLYCOSYL HYDROLASES
ORGANIC COMPOUNDS
PLANTS
RECOMBINANT DNA
SYNTHESIS
TRICHODERMA