Please use this identifier to cite or link to this item: http://hdl.handle.net/2440/11426
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Type: Journal article
Title: Molecular characterisation of mutants of the acetate regulatory gene facB of Aspergillus nidulans
Author: Todd, R.
Kelly, J.
Davis, M.
Hynes, M.
Citation: Fungal Genetics and Biology, 1997; 22(2):92-102
Issue Date: 1997
ISSN: 1087-1845
1096-0937
Abstract: The facB gene of Aspergillus nidulans encodes a DNA binding transcriptional activator required for growth on acetate as a sole carbon source. FacB contains N-terminal GAL4-like Zn(II)2Cys6 (or C6 zinc) binuclear cluster DNA binding and leucine zipper-like heptad repeat motifs and central and C-terminal acidic alpha-helical regions. facB recessive loss of function mutants are deficient in acetate induction of acetyl-CoA synthase, isocitrate lyase, malate synthase, acetamidase, and NADP-isocitrate dehydrogenase. Characterization of lesions in facB mutant alleles has localized important functional regions of the FacB protein. Two extreme mutants are shown to lack the C-terminal region of the protein. Two temperature sensitive mutants contain amino acid substitutions in the DNA binding domain and are shown to affect acetate induction of amdS-lacZ expression and confer temperature sensitive in vitro DNA binding. Two temperature sensitive facB mutations result in thermolability of acetyl-CoA synthase, isocitrate lyase, and malate synthase but not acetamidase or NADP-isocitrate dehydrogenase in crude extracts. This suggests that FacB may have a structural role in acetate metabolism in addition to its regulatory function.
Keywords: Escherichia coli; Aspergillus nidulans; Acetates; Amidohydrolases; Trans-Activators; Fungal Proteins; Recombinant Fusion Proteins; Sequence Analysis, DNA; Enzyme Stability; Temperature; Enzyme Induction; Sequence Deletion; Amino Acid Sequence; Zinc Fingers; Mutation; Alleles; Genes, Fungal; Molecular Sequence Data
RMID: 0030004322
DOI: 10.1006/fgbi.1997.1007
Appears in Collections:Genetics publications

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