Cloning and functional characterization of the gene encoding the transcription factor Acel in the basidiomycete Phanerochaete chrysosporium

Polanco, Rubén; Canessa, Paulo; Rivas, Alexis; Larrondo, Luis F.; Lobos, Sergio; Vicuña, Rafael

doi:10.4067/s0716-97602006000500007

Cited by 15 publications

(30 citation statements)

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“…This metal is essential for the DNAbinding activity of ACE1 (Winge, 1998). Interestingly, we have recently identified the gene encoding ACE1 in P. chrysosporium (Pc-ace1), the first basidiomycetal orthologue of the yeast ACE1 transcription factor (Polanco et al, 2006). However, until this work, the possible target gene(s) of Pc-ACE1 remained unknown.…”

Section: Introductionmentioning

confidence: 95%

“…The fact that copper affects the transcription of various MCO-encoding genes in different organisms, plus the presence of putative ACE elements in the promoter of mco1 (Polanco et al, 2006), led us to analyse the effect of copper on the expression of this novel group of multicopper oxidases recently discovered in P. chrysosporium (Larrondo et al, 2003). In this work we show that mco1 is a target gene of the recently described ACE1 transcription factor in P. chrysosporium.…”

Section: Introductionmentioning

confidence: 98%

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The copper-dependent ACE1 transcription factor activates the transcription of the mco1 gene from the basidiomycete Phanerochaete chrysosporium

et al. 2008

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We have previously identified and functionally characterized the transcription factor ACE1 (Pc-ACE1) from Phanerochaete chrysosporium. In Saccharomyces cerevisiae, ACE1 activates the copper-dependent transcription of target genes through a DNA sequence element named ACE. However, the possible target gene(s) of Pc-ACE1 were unknown. An in silico search led to the identification of putative ACE elements in the promoter region of mco1, one of the four clustered genes encoding multicopper oxidases (MCOs) in P. chrysosporium. Since copper exerts an effect at the transcriptional level in MCOs from several organisms, in this work we analysed the effect of copper on transcript levels of the clustered MCO genes from P. chrysosporium, with the exception of the transcriptionally inactive mco3. Copper supplementation of cultures produced an increment in transcripts from genes mco1 and mco2, but not from mco4. Electrophoretic mobility-shift assays revealed that Pc-ACE1 binds specifically to a probe containing one of the putative ACE elements found in the promoter of mco1. In addition, using a cell-free transcription system, we showed that in the presence of cuprous ion, Pc-ACE1 induces activation of the promoter of mco1, but not that of mco2.

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Section: Introductionmentioning

confidence: 95%

Section: Introductionmentioning

confidence: 98%

The copper-dependent ACE1 transcription factor activates the transcription of the mco1 gene from the basidiomycete Phanerochaete chrysosporium

et al. 2008

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“…White-rot fungi have the ability to break down lignin, a highly recalcitrant polymer present in plant cell walls (Polanco et al 2006). Extracellular enzymes involved in lignin degradation are mainly peroxidases, such as lignin peroxidase (LiP, E.C.…”

Section: Influence Of Culture Conditions On Laccase Production Growtmentioning

confidence: 99%

Influence of Culture Conditions on Laccase Production, Growth, and Isoenzymes Patterns in Native White Rot Fungi from the Misiones Rainforest (Argentina)

et al. 2013

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aMany biotechnological processes pursuing sustainability aim for effective, inexpensive, and environmentally friendly alternatives to replace conventional practices. Laccase-containing lignocellulolytic systems from white rot fungi have been shown to be an efficient enzymatic tool for ecofriendly biological treatments. One objective of the biotechnological enzymes production process is to find optimum growing and secretion conditions for a selected fungus. In this work, different fungi isolated from the Misiones rainforest (Coriolus versicolor f. antarcticus BAFC-266, Ganoderma applanatum strain F, Phlebia brevispora BAFC-633, and Pycnoporus sanguineus BAFC-2126) were incubated at different temperatures (25, 29, 33 °C) and pH values (3.5, 4.5, 5.5) under static conditions for 7, 10, and 14 days to evaluate their growing ability and laccase (Lac) production. Results revealed specific favorable conditions for growth and protein secretion depending on the fungus under consideration, making it necessary to adjust these parameters for each particular case. The combined effect of these cultivation parameters showed a marked influence on the secreted Lac activity by P. brevispora BAFC 633, with the highest activity (~ 240 U/l) at 29 ºC and pH 4.5 at the 10 th day of cultivation. The presence of Lac isoenzymes also depended on the pH, temperature, and time of cultivation for the different tested fungi.

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“…Functionally, it is the ortholog of Ace1 from Saccharomyces cerevisiae. This was demonstrated by complementation assays using a S. cerevisiae ace1Δ strain, in which the capacity of this mutant to grow at high copper concentration was restored when PcACE1 cDNA was introduced (Polanco et al, 2006). Moreover, in vitro transcribed and translated PcACE1 protein was able to bind in a gel-shift assay to the promoter of the yeast metallothionein in the presence of copper, but not in its absence (Canessa et al, 2008).…”

Section: Introductionmentioning

confidence: 88%

“…It was cloned by Polanco et al (2006) and is activated when copper concentration is high. Functionally, it is the ortholog of Ace1 from Saccharomyces cerevisiae.…”

Section: Introductionmentioning

confidence: 99%

The PcACE1 transcription factor from Phanerochaete chrysosporium contains a Cys- and Ser-rich transactivation domain

2011

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Transcription factor Ace1 from Saccharomyces cerevisiae regulates the expression of target genes when the copper concentration reaches 200 μM levels. We are studying the ortholog of Ace1 from fungus Phanerochaete chrysosporium PcACE1, isolated by complementation in yeast. In this report we show the localization of the transactivation region of PcACE1. Different PcACE1 fragments were ligated in frame to the GAL4 DNA-binding domain by site-directed mutagenesis in a suitable yeast expression vector. Transformation of an appropriate Saccharomyces cerevisiae strain was used as host. This strain contains the fusion GAL1:lacZ in its genome under the control of promoter sequences recognized by GAL4. Finally, we measured β-galactosidase activity in each yeast clone. The activation of the reporter gene is proportional to the transactivation capacity of the transcription factor PcACE1. The results obtained indicate that PcACE1 transactivation domain is located in the carboxy terminal half and contains an array of cysteines in the form of Cys-X-Cys and Cys-X 2 -Cys and a 60% of Ser. Therefore, these results show that this type of Cys motif can function as transcription activating domain not only in transcription factors that respond to minimal copper concentrations but also in those that respond to high copper concentrations. This is the fi rst transactivation domain reported in a basidiomycete fungus.

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Cloning and functional characterization of the gene encoding the transcription factor Acel in the basidiomycete Phanerochaete chrysosporium

Cited by 15 publications

References 26 publications

The copper-dependent ACE1 transcription factor activates the transcription of the mco1 gene from the basidiomycete Phanerochaete chrysosporium

The copper-dependent ACE1 transcription factor activates the transcription of the mco1 gene from the basidiomycete Phanerochaete chrysosporium

Influence of Culture Conditions on Laccase Production, Growth, and Isoenzymes Patterns in Native White Rot Fungi from the Misiones Rainforest (Argentina)

The PcACE1 transcription factor from Phanerochaete chrysosporium contains a Cys- and Ser-rich transactivation domain

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