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Carbon catabolite repression in Aspergillus nidulans involves deubiquitination
1Department of Molecular Biosciences, University of Adelaide, Adelaide, SA 5005, Australia.
Molecular Microbiology
|July 10, 2001
Summary
Ubiquitination regulates carbon catabolite repression in Aspergillus nidulans. The CreB protein, a deubiquitinating enzyme, plays a key role in this process, alongside the CreC protein.
Area of Science:
- Molecular Biology
- Biochemistry
- Genetics
Background:
- Ubiquitination primarily marks proteins for proteasomal degradation.
- Emerging roles of ubiquitination include regulating macromolecular assembly, function, and protein activity.
- Deubiquitinating enzymes (DUBs), such as ubiquitin-processing proteases (UBPs) and ubiquitin carboxy-terminal hydrolases (UCHs), remove ubiquitin from substrates.
Purpose of the Study:
- To investigate the role of ubiquitination in carbon catabolite repression.
- To identify novel deubiquitinating enzymes involved in this regulatory pathway.
Main Methods:
- Genetic analysis of Aspergillus nidulans mutants.
- Characterization of the creB gene and its protein product.
- Phenotypic analysis of mutant strains.
Main Results:
- The creB gene in Aspergillus nidulans encodes a functional deubiquitinating enzyme belonging to a novel UBPs subfamily.
- This subfamily, including human UBH1 homologues, is conserved across eukaryotes.
- Mutations in creB and creC genes result in identical phenotypes, suggesting their involvement in a shared regulatory pathway.
Conclusions:
- Ubiquitination is implicated in the regulation of carbon catabolite repression.
- The novel UBPs subfamily, represented by CreB, plays a significant role in complex regulatory pathways.
- CreB and CreC function together in a pathway critical for carbon catabolite repression in Aspergillus nidulans.