The DNA-binding domain of the Cys-3 regulatory protein of Neurospora crassa is bipartite

Kanaan, Moien; Fu, Ying Hui; Marzluf, George A.

doi:10.1021/bi00127a022

Cited by 16 publications

(5 citation statements)

References 22 publications

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“…A lysine residue found in the d position of the fourth FacB heptad repeat is uncommon in a-helical coiled coils, but lysine has been observed in this position in a-®brous proteins (Cohen and Parry 1990). The heptad repeats of FacB show strong homology to those of the well-characterised leucine zipper of the N. crassa Cys3 protein, which favour homodimerization rather than heterodimerization (Kanaan and Marzluf 1991;Kanaan et al 1992;Paietta 1995).…”

Section: Discussionmentioning

confidence: 99%

“…The heptad repeats of FacB are leucine zipperlike in that leucine residues predominate at the d position (Landshulz et al 1988;Cohen and Parry 1990). The FacB heptad repeats show similarity to the heptad repeat region of CAT8 (Hedges et al 1995) and the leucine zipper region of the N. crassa Cys-3 protein (Fu et al 1989), which is involved in dimerization (Kanaan and Marzluf 1991;Kanaan et al 1992;Paietta 1995;see Fig. 2b).…”

Section: Structure Of the Predicted Facb Proteinmentioning

confidence: 99%

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The acetate regulatory gene facB of Aspergillus nidulans encodes a Zn(II)2Cys6 transcriptional activator

et al. 1997

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Genetic studies have indicated that the facB gene of Aspergillus nidulans is a major regulatory gene involved in acetamide and acetate utilisation. Sequencing of the facB gene revealed that it encodes a protein that contains an N-terminal GAL4-like Zn(II)2Cys6 (or C6 zinc) binuclear cluster for DNA binding, leucine zipper-like heptad repeat motifs and central and C-terminal acidic alpha-helical regions, consistent with a function as a DNA-binding transcriptional activator. The Zn(II)2Cys6 cluster shows strong similarity with those of the Saccharomyces cerevisiae carbon metabolism regulatory proteins CAT8 and SIP4. A significant level of similarity with CAT8 is found throughout the length of the protein, suggesting at least partial functional homology. The facB genes of Aspergillus oryzae and Aspergillus niger were also sequenced and found to be highly conserved. Deletion of the facB gene confirmed that it is required for growth on acetate as a sole carbon source. Functional dissection using deletion and fusion constructs and in vitro mutagenesis indicated that the Zn(II)2Cys6 cluster and the C-terminal end of the protein are required for function.

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Section: Discussionmentioning

confidence: 99%

Section: Structure Of the Predicted Facb Proteinmentioning

confidence: 99%

The acetate regulatory gene facB of Aspergillus nidulans encodes a Zn(II)2Cys6 transcriptional activator

et al. 1997

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“…CYS3 is a member of the bZlP protein family of DNA-binding factors. The leucine zipper and basic region of CYSB mediate dimerization and specific contacts with DNA, respectively (Kanaan et a/., 1992). The CYS3 protein recognizes the consensus sequence 5' ATGPuPyPuPyCAT-3', which resembles an ATF/CREB site.…”

Section: Introductionmentioning

confidence: 99%

Functional in vivo studies of the Neurospora crassa cys‐14 gene upstream region: importance of CYS3‐binding sites for regulated expression

Zhou

Marzluf

1996

Molecular Microbiology

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Sulphate transport in Neurospora crassa is achieved by two distinct sulphate permeases, I and II, encoded by the cys-13 and cys-14 genes, respectively. The synthesis of both sulphate permeases is subject to sulphur repression and requires the global positive-acting regulatory protein CYS3, CYS3, a bZIP DNA binding protein, regulates cys-14 expression at the transcriptional level and binds in vitro specifically to three DNA-recognition sites, A, B, and C, in the cys-14 upstream region. In vivo functional analysis of the cys-14 promoter was carried out with 5' deletions and by deletions or mutations of CYS3 DNA-binding sites. The most distal CYS3-binding site, C, located 1.4kb upstream of the transcriptional start site, is necessary and sufficient to mediate strong transcriptional activation by CYS3; moreover, site C was able to function equally well when it was located at variable distances upstream of the cys-14 gene. Site B, located 1 kb upstream, alone is able to support a moderate degree of cys-14 expression. Site A is not required and does not appear to play any functional role in cys-14 expression, even though it is in close proximity to the transcriptional start site. The presence of multiple copies of CYS3-binding elements A or B in the cys-14 promoter results in a parallel increase of regulated gene expression. When a transforming cys-14 gene becomes integrated at ectopic locations in the host genome, it can be expressed in an unregulated fashion, presumably by coming under the control of other promoter elements. Our results also suggested that at least one enzyme in the sulphate catabolic pathway requires a functional CYS3 protein for expression.

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“…CYS3 functions as a homodimer (Kanaan et al 1992) and recognizes the palindromic sequence 5-ATGRYRYCAT-3 (Li and Marzluf 1996) present in promoters of sulfur assimilation genes (Fu and Marzluf 1990;Fu et al 1989). In Aspergillus nidulans, an ortholog of CYS3 is MetR activating transcription of sulfur metabolism genes, in particular those involved in sulfate assimilation (Natorff et al 2003).…”

Section: Introductionmentioning

confidence: 99%

The Aspergillus nidulans metZ gene encodes a transcription factor involved in regulation of sulfur metabolism in this fungus and other Eurotiales

et al. 2014

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In Aspergillus nidulans, expression of sulfur metabolism genes is activated by the MetR transcription factor containing a basic region and leucine zipper domain (bZIP). Here we identified and characterized MetZ, a new transcriptional regulator in A. nidulans and other Eurotiales. It contains a bZIP domain similar to the corresponding region in MetR and this similarity suggests that MetZ could potentially complement the MetR deficiency. The metR and metZ genes are interrupted by unusually long introns. Transcription of metZ, unlike that of metR, is controlled by the sulfur metabolite repression system (SMR) dependent on the MetR protein. Overexpression of metZ from a MetR-independent promoter in a ΔmetR background activates transcription of genes encoding sulfate permease, homocysteine synthase and methionine permease, partially complementing the phenotype of the ΔmetR mutation. Thus, MetZ appears to be a second transcription factor involved in regulation of sulfur metabolism genes.

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The DNA-binding domain of the Cys-3 regulatory protein of Neurospora crassa is bipartite

Cited by 16 publications

References 22 publications

The acetate regulatory gene facB of Aspergillus nidulans encodes a Zn(II)2Cys6 transcriptional activator

The acetate regulatory gene facB of Aspergillus nidulans encodes a Zn(II)2Cys6 transcriptional activator

Functional in vivo studies of the Neurospora crassa cys‐14 gene upstream region: importance of CYS3‐binding sites for regulated expression

The Aspergillus nidulans metZ gene encodes a transcription factor involved in regulation of sulfur metabolism in this fungus and other Eurotiales

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