Analysis of the creA gene, a regulator of carbon catabolite repression in Aspergillus nidulans.

Dowzer, C. E. A.; Kelly, Joseph F.

doi:10.1128/mcb.11.11.5701

Cited by 341 publications

(260 citation statements)

References 43 publications

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“…Growth on decreasing concentrations of glucose for 20 hr resulted in increased expression ( Figure 4B). The creA gene in A. nidulans encodes a repressor protein with two C2H2 zinc fingers similar to those of S. cerevisiae Mig1p and is required for carbon catabolite repression (Dowzer and Kelly 1991). The creA204 mutation in the DNA-binding domain results in loss of glucose repression (Shroff et al 1996).…”

Section: Resultsmentioning

confidence: 99%

Transcriptional Control of Gluconeogenesis in Aspergillus nidulans

et al. 2007

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Aspergillus nidulans can utilize carbon sources that result in the production of TCA cycle intermediates, thereby requiring gluconeogenesis. We have cloned the acuG gene encoding fructose-1,6 bisphosphatase and found that expression of this gene is regulated by carbon catabolite repression as well as by induction by a TCA cycle intermediate similar to the induction of the previously studied acuF gene encoding phosphoenolpyruvate carboxykinase. The acuN356 mutation results in loss of growth on gluconeogenic carbon sources. Cloning of acuN has shown that it encodes enolase, an enzyme involved in both glycolysis and gluconeogenesis. The acuN356 mutation is a translocation with a breakpoint in the 59 untranslated region resulting in loss of expression in response to gluconeogenic but not glycolytic carbon sources. Mutations in the acuK and acuM genes affect growth on carbon sources requiring gluconeogenesis and result in loss of induction of the acuF, acuN, and acuG genes by sources of TCA cycle intermediates. Isolation and sequencing of these genes has shown that they encode proteins with similar but distinct Zn(2) Cys(6) DNA-binding domains, suggesting a direct role in transcriptional control of gluconeogenic genes. These genes are conserved in other filamentous ascomycetes, indicating their significance for the regulation of carbon source utilization.

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Section: Resultsmentioning

confidence: 99%

Transcriptional Control of Gluconeogenesis in Aspergillus nidulans

et al. 2007

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“…CreA has been identified in A. nidulans as a GC-box binding repressor involved in glucose repression (Arst & MacDonald, 1975 ;Dowzer & Kelly, 1991 ;Strauss et al, 1999). This glucose effect -repression of genes that are used in the metabolism of alternative carbon sources -is widely known in fungi and yeasts (Ronne, 1995).…”

Section: Discussionmentioning

confidence: 99%

Characterization of the major laccase isoenzyme from Trametes pubescens and regulation of its synthesis by metal ions a aThe GenBank accession numbers for the lap2 and lap1a genes reported in this paper are AF414807 and AF414808, respectively.

et al. 2002

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The major laccase isoenzyme LAP2 secreted by the white-rot basidiomycete Trametes pubescens in response to high copper concentrations was purified to apparent electrophoretic homogeneity using anion-exchange chromatography and gel filtration. The monomeric protein has a molecular mass of 65 kDa, of which 18 % is glycosylation, and a pI value of 2 6. The pH optima of the laccase depend on the substrates oxidized and show bell-shaped pH activity profiles with an optimum of 3-4 5 for phenolic substrates such as 2,6-dimethoxyphenol or syringaldazine, while the non-phenolic substrates ABTS [2,2'-azino-bis(3-ethylbenzthiazoline-6-sulfonic acid)] and ferrocyanide show a monotonic pH profile with a rate increasing with decreasing pH. The catalytic efficiencies k cat /K m determined for some of its substrates were 48W10 6 , 47W10 6 , 20W10 6 and 7W10 6 M N1 s N1 for ABTS, syringaldazine, ferrocyanide and oxygen, respectively. Furthermore, the gene lap2 encoding the purified laccase was cloned and its nucleotide sequence determined. The gene consists of 1997 bp, with the coding sequence interrupted by eight introns and flanked by an upstream region in which putative CAAT, TATA, MRE and CreA consensus sequences were identified. Based on Northern analysis containing total RNA from both induced and uninduced cultures, expression of lap2 is highly induced by copper, which is also corroborated by an increase in laccase activity in response to copper. A stimulating effect of various other heavy metal ions on laccase synthesis was also observed. In addition to induction, a second regulatory mechanism seems to be repression of lap2 transcription by glucose.

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“…The potential involvement of nitrogen metabolism in amylase production was assessed. It is another mode of the amylase enzyme expression system, which is different from the conventional mode previously explained for AmyR [12][13][14] and CreA, 15,16) and in another aspect different from the glycogen-related metabolism in the mycelia. 17,18) On the basis of the above-described assessment results, the following hypothesis that might explain the high enzyme production by A. oryzae in the submerged culture with UWB was considered: First, in the first half of the period of culture using MWB, rapid glucose release from the raw material owing to milling activates glycolysis.…”

Section: Gene Expression Analysismentioning

confidence: 99%

Analysis of Enzyme Production by Submerged Culture ofAspergillus oryzaeUsing Whole Barley

Masuda

Kikuchi

Matsumoto

et al. 2009

Bioscience, Biotechnology, and Biochemistry

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Analysis of the creA gene, a regulator of carbon catabolite repression in Aspergillus nidulans.

Abstract: The complete nucleotide sequence derived from a genomic clone and two cDNA clones of the creA gene

Cited by 341 publications

References 43 publications

Transcriptional Control of Gluconeogenesis in Aspergillus nidulans

Transcriptional Control of Gluconeogenesis in Aspergillus nidulans

Characterization of the major laccase isoenzyme from Trametes pubescens and regulation of its synthesis by metal ions a aThe GenBank accession numbers for the lap2 and lap1a genes reported in this paper are AF414807 and AF414808, respectively.

Analysis of Enzyme Production by Submerged Culture ofAspergillus oryzaeUsing Whole Barley

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