The tamA gene of Aspergillus nidulans contains a putative zinc cluster motif which is not required for gene function

Davis, Meryl A.; Small, Anna J.; Kourambas, Sophie; Hynes, Michael J.

doi:10.1128/jb.178.11.3406-3409.1996

Cited by 40 publications

(45 citation statements)

References 36 publications

(34 reference statements)

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“…LeuB, a homolog of S. cerevisiae Leu3, and TamA are both involved in controlling the expression of the gdhA gene encoding NADP-linked glutamate dehydrogenase. Moreover, mutating a critical cysteine residue in the zinc cluster domain of TamA has no effect on its functionality (Davis et al 1996). Thus, results suggest that the DNA-binding domain of Dal81 and TamA are dispensable in spite of the fact that the primary amino acid sequence of the cysteine-rich region of these factors corresponds to a bona fide zinc cluster.…”

Section: Discussionmentioning

confidence: 68%

“…It therefore appears that the zinc cluster motif of Dal81 is not required for the activation of at least some of its target genes. A similar observation was made for TamA, a protein found in the filamentous fungus Aspergillus nidulans, which is also required for the activation of genes involved in the catabolism of nitrogen sources such as GABA (Davis et al 1996;Small et al 2001).…”

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confidence: 82%

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Yeast Zinc Cluster Proteins Dal81 and Uga3 Cooperate by Targeting Common Coactivators for Transcriptional Activation of Γ-Aminobutyrate Responsive Genes

Sylvain¹,

Liang²,

Hellauer³

et al. 2011

Genetics

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In Saccharomyces cerevisiae, optimal utilization of various compounds as a nitrogen source is mediated by a complex transcriptional network. The zinc cluster protein Dal81 is a general activator of nitrogen metabolic genes, including those for g-aminobutyrate (GABA). In contrast, Uga3 (another zinc cluster protein) is an activator restricted to the control of genes involved in utilization of GABA. Uga3 binds to DNA elements found in the promoters of target genes and increases their expression in the presence of GABA. Dal81 appears to act as a coactivator since the DNA-binding activity of this factor is dispensable but its mode of action is not known. In this study, we have mapped a regulatory, as well as an activating, region for Uga3. A LexA-Uga3 chimeric protein activates a lexA reporter in a GABA-and Dal81-dependent manner. Activation by Uga3 requires the SAGA complex as well as Gal11, a component of mediator. ChIP analysis revealed that Uga3 is weakly bound to target promoters. The presence of GABA enhances binding of Uga3 and allows recruitment of Dal81 and Gal11 to target genes. Recruitment of Gal11 is prevented in the absence of Dal81. Importantly, Dal81 by itself is a potent activator when tethered to DNA and its activity depends on SAGA and Gal11 but not Uga3. Overexpression of Uga3 bypasses the requirement for Dal81 but not for SAGA or Gal11. Thus, under artificial conditions, both Dal81 and Uga3 can activate transcription independently of each other. However, under physiological conditions, both factors cooperate by targeting common coactivators.

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Section: Discussionmentioning

confidence: 68%

mentioning

confidence: 82%

Yeast Zinc Cluster Proteins Dal81 and Uga3 Cooperate by Targeting Common Coactivators for Transcriptional Activation of Γ-Aminobutyrate Responsive Genes

Sylvain¹,

Liang²,

Hellauer³

et al. 2011

Genetics

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“…Similar observations were made for the A. nidulans protein TamA, a protein closely related to Dal81 that is involved in nitrogen utilization (Davis et al, 1996). So, we wondered whether the Zn(II) 2 -Cys 6 domain and also the polyglutamine streeches (residues 73-94 and 227-237) present in the Dal81 protein were required for GABA induction of UGA regulon genes.…”

Section: Dal81 Transcription Factor Is Necessary For Uga3 Binding To mentioning

confidence: 66%

“…This domain is essential for Uga3 activity (Talibi et al, 1995). However, Dal81, like Aspergillus nidulans TamA, does not require the Zn(II) 2 -Cys 6 domain to fully activate the DUR1/ 2 gene (Bricmont et al, 1991;Davis et al, 1996).…”

Section: Introductionmentioning

confidence: 99%

Interplay between the transcription factors acting on the GATA- and GABA-responsive elements of Saccharomyces cerevisiae UGA promoters

et al. 2012

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c-Aminobutyric acid (GABA) transport and catabolism in Saccharomyces cerevisiae are subject to a complex transcriptional control that depends on the nutritional status of the cells. The expression of the genes that form the UGA regulon is inducible by GABA and sensitive to nitrogen catabolite repression (NCR). GABA induction of these genes is mediated by Uga3 and Dal81 transcription factors, whereas GATA factors are responsible for NCR. Here, we show how members of the UGA regulon share the activation mechanism. Our results show that both Uga3 and Dal81 interact with UGA genes in a GABA-dependent manner, and that they depend on each other for the interaction with their target promoters and the transcriptional activation. The typical DNA-binding domain Zn(II) 2 -Cys 6 of Dal81 is unnecessary for its activity and Uga3 acts as a bridge between Dal81 and DNA. Both the trans-activation activity of the GATA factor Gln3 and the repressive activity of the GATA factor Dal80 are exerted by their interaction with UGA promoters in response to GABA, indicating that Uga3, Dal81, Gln3 and Dal80 all act in concert to induce the expression of UGA genes. So, an interplay between the factors responsible for GABA induction and those responsible for NCR in the regulation of the UGA genes is proposed here.

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“…At least two known zinc cluster proteins do not require the cysteine-rich DBD. Both S. cerevisiae Dal81p and Aspergillus nidulans TamAp proteins appear fully functional when their zinc clusters are deleted or disrupted (25,49).…”

Section: Structural and Functional Domainsmentioning

confidence: 99%

A Fungal Family of Transcriptional Regulators: the Zinc Cluster Proteins

MacPherson¹,

Larochelle²,

Turcotte

2006

Microbiol Mol Biol Rev

504

554

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SUMMARY The trace element zinc is required for proper functioning of a large number of proteins, including various enzymes. However, most zinc-containing proteins are transcription factors capable of binding DNA and are named zinc finger proteins. They form one of the largest families of transcriptional regulators and are categorized into various classes according to zinc-binding motifs. This review focuses on one class of zinc finger proteins called zinc cluster (or binuclear) proteins. Members of this family are exclusively fungal and possess the well-conserved motif CysX2CysX6CysX5-12CysX2CysX6-8Cys. The cysteine residues bind to two zinc atoms, which coordinate folding of the domain involved in DNA recognition. The first- and best-studied zinc cluster protein is Gal4p, a transcriptional activator of genes involved in the catabolism of galactose in the budding yeast Saccharomyces cerevisiae. Since the discovery of Gal4p, many other zinc cluster proteins have been characterized; they function in a wide range of processes, including primary and secondary metabolism and meiosis. Other roles include regulation of genes involved in the stress response as well as pleiotropic drug resistance, as demonstrated in budding yeast and in human fungal pathogens. With the number of characterized zinc cluster proteins growing rapidly, it is becoming more and more apparent that they are important regulators of fungal physiology.

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The tamA gene of Aspergillus nidulans contains a putative zinc cluster motif which is not required for gene function

Cited by 40 publications

References 36 publications

Yeast Zinc Cluster Proteins Dal81 and Uga3 Cooperate by Targeting Common Coactivators for Transcriptional Activation of Γ-Aminobutyrate Responsive Genes

Yeast Zinc Cluster Proteins Dal81 and Uga3 Cooperate by Targeting Common Coactivators for Transcriptional Activation of Γ-Aminobutyrate Responsive Genes

Interplay between the transcription factors acting on the GATA- and GABA-responsive elements of Saccharomyces cerevisiae UGA promoters

A Fungal Family of Transcriptional Regulators: the Zinc Cluster Proteins

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