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FacB, the Aspergillus nidulans activator of acetate utilization genes, binds dissimilar DNA sequences
Author(s) -
Todd Richard B.,
Andrianopoulos Alex,
Davis Meryl A.,
Hynes Michael J.
Publication year - 1998
Publication title -
the embo journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 7.484
H-Index - 392
eISSN - 1460-2075
pISSN - 0261-4189
DOI - 10.1093/emboj/17.7.2042
Subject(s) - aspergillus nidulans , biology , gene , activator (genetics) , dna , aspergillus , genetics , fungal protein , microbiology and biotechnology , biochemistry , peptide sequence , mutant
The facB gene is required for acetate induction of acetamidase ( amdS ) and the acetate utilization enzymes acetyl‐CoA synthase ( facA ), isocitrate lyase ( acuD ) and malate synthase ( acuE ) in Aspergillus nidulans . The facB gene encodes a transcriptional activator with a GAL4‐type Zn(II)2Cys6 zinc binuclear cluster DNA‐binding domain which is shown to be required for DNA binding. In vitro DNA‐binding sites for FacB in the 5′ regions of the amdS , facA , acuD and acuE genes have been identified. Mutations in amdS FacB DNA‐binding sites affected expression of an amdS–lacZ reporter in vivo and altered the affinity of in vitro DNA binding. This study shows that the FacB Zn(II)2Cys6 cluster binds to dissimilar sites which show similarity in form but not sequence with DNA‐binding sites of other Zn(II)2Cys6 proteins. Sequences with homology to FacB sites are found in the 5′ regions of genes regulated by the closely related yeast Zn(II)2Cys6 protein CAT8.