Gene/Protein
Disease
Symptom
Drug
Enzyme
Compound
Pivot Concepts:
Gene/Protein
Disease
Symptom
Drug
Enzyme
Compound
Target Concepts:
Gene/Protein
Disease
Symptom
Drug
Enzyme
Compound
Query: UNIPROT:P51532 (
transcriptional activator
)
6,546
document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)
Enzymes that degrade lignocellulose to simple sugars are of great interest in research and for biotechnology because of their role in converting plant biomass to fuels and chemicals. The synthesis of cellulolytic enzymes in filamentous fungi is tightly regulated at the transcriptional level, with the
transcriptional activator
ClrB/CLR-2 playing a critical role in many species. In
Penicillium oxalicum
,
clrB
overexpression could not relieve the dependence of cellulase expression on cellulose as an inducer, suggesting that
clrB
is controlled post-transcriptionally. In this study, using a reporter gene system in yeast, we identified the C-terminal region of ClrB/CLR-2 as a transcriptional activation domain. Expression of
clrB
ID
, encoding a ClrB derivative in which the DNA-binding and transcriptional activation domains are fused together to remove the middle region, led to cellulase production in the absence of cellulose in
P. oxalicum
Strikingly, the
clrB
ID
-expressing strain produced cellulase on carbon sources that normally repress cellulase expression, including glucose and glycerol. Results from deletion of the carbon catabolite repressor gene
creA
in the
clrB
ID
-expressing strain suggested that the effect of
clrB
ID
is independent of CreA's repressive function. A similar modification of
clrB
in
Aspergillus niger
resulted in the production of a
mannanase
in glucose medium. Taken together, these results indicate that ClrB suppression under noninducing conditions involves its middle region, suggesting a potential strategy to engineer fungal strains for improved cellulase production on commonly used carbon sources.
...
PMID:Deletion of the middle region of the transcription factor ClrB in
Penicillium oxalicum
enables cellulase production in the presence of glucose. 3165 20
