Cloning and sequencing of a laccase gene from the lignin-degrading basidiomycete Pleurotus ostreatus

Giardina, Paola; Cannio, Raffaele; Martirani, Luca; Marzullo, Liberato; Palmieri, Gianna; Sannia, Giovanni

doi:10.1128/aem.61.6.2408-2413.1995

Cited by 125 publications

(52 citation statements)

References 31 publications

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“…A number of other putative response elements, including MRE (TGC(G/A)CNC) and XRE (TCACGC) have also been identified in promoter regions of different white-rot fungal laccase and manganese peroxidase genes (Coll et al 1993;Gold and Alic 1993;Giardina et al 1995). MRE are typically found in metallothionein gene promoters in higher eukaryotes (Imbert et al 1990), with expression being induced by heavy metal ions such as Cd, Cu and Zn (Hamer 1995).…”

Section: Discussionmentioning

confidence: 99%

The use of amplified flanking region-PCR in the isolation of laccase promoter sequences from the edible fungus Pleurotus sajor-caju

Soden¹,

Dobson

2003

J Appl Microbiol

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Aims: To determine the regulation of laccase isozyme gene transcription in Pleurotus sajor-caju in response to different aromatic inducers and physiological parameters. Methods and Results: The promoter regions for each of four different laccase isozymes were cloned from P. sajor-caju, using amplified flanking region-PCR (AFR-PCR). Sequences stretching 724, 214, 840 and 1740 bp upstream from the predicted start codons for lac1, lac2, lac3 and lac4, respectively, were cloned in each case and analysed for the presence of putative transcriptional response elements. A number of putative response elements including metal response elements, xenobiotic response elements and antioxidant response elements appear to be present. In addition putative consensus sequences such as those for the binding of AP1, AP2, creA and NIT2 transcription factors, which are involved in nitrogen and carbon regulation in different fungi, are also present in the promoter regions of some of the isozymes. Conclusions: These elements may be involved in the transcriptional regulation of laccase gene expression in P. sajor-caju. Significance and Impact of the Study: The presence of a number of putative transcriptional response elements in the promoter regions of different isozyme genes indicates a potential role for these sites in regulating laccase gene transcription in P. sajor-caju. In addition this work demonstrates the potential usefulness of AFR-PCR as a technique to clone fungal DNA sequences located upstream from known sequences.

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Section: Discussionmentioning

confidence: 99%

The use of amplified flanking region-PCR in the isolation of laccase promoter sequences from the edible fungus Pleurotus sajor-caju

Soden¹,

Dobson

2003

J Appl Microbiol

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“…Fungal laccases, as blue copper oxidases have three types of copper atoms ; the type 1 (or blue copper) site is responsible for the intensive blue color of the enzyme, type 2 and type 3 copper sites give almost no absorbance in the visible range [24]. CLAC2 has only two copper binding regions I and II, where type 1 copper does not bind [14,25], and that is why CLAC2 shows no blue color (no absorbance at red light range) [26]. P. ostreatus has many di¡erent laccases, and a white laccase POXA1 has one copper atom with two zinc and one iron [27].…”

Section: Discussionmentioning

confidence: 99%

Cloning of an acidic laccase gene (clac2) from Coprinus congregatus and its expression by external pH

Kim

2001

FEMS Microbiology Letters

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Coprinus congregatus synthesized and secreted high amounts of laccase under acidic culture condition (pH 4.1) transiently. We have cloned a genomic DNA fragment between the copper binding regions I and II of a laccase by PCR from C. congregatus. This fragment was used as a probe to clone a laccase cDNA from the acidic culture. The cDNA (clac2) consisted of 1817 bp which contains 1086 bp encoding 362 amino acids. The N-terminal sequence of the purified CLAC2 revealed that the first 16 amino acids were removed by the modification. The purified protein had two copper binding regions, although other fungal laccases had four. According to a Northern blotting analysis the clac2 was expressed not in neutral culture but in acidic culture only. The transcription of the clac2 as well as the laccase activity reached a maximum after 24 h upon transferring to an acidic culture, and then decreased very rapidly. ß

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“…Laccase is an enzyme which is widely distributed in many genera of white rot fungi (BOLLAG et al 1988, GIARDINA et al 1995, MAYER 1987, SANNIA et al 1986, THURSTON 1994, YOUN et al 1995. However, the biological functions of the enzyme in the producer organisms are not clear (MAYER 1987, THURSTON 1994.…”

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confidence: 99%

Purification and characterization of a growth-regulating laccase from Pleurotus florida

Das¹,

Chakraborty²,

Mukherjee³

2001

J. Basic Microbiol.

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Pleurotus florida produces two laccase enzymes (L1 and L2) within which L2 is associated with the vegetative growth of the fungus. In the present investigation the L2 has been purified to homogeneity and characterized. The molecular mass of the enzyme has been determined to be 73 kDa and 70 kDa by gel filtration chromatography and SDS‐PAGE, respectively. The purified enzyme shows a pI value of 4.2. The optimum reaction temperature is 50 °C. Spectroscopic analysis reveals that L2 has two copper atoms, a type I copper and a type II copper. The Km and some other kinetic parameters of L2 has been determined.

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Cloning and sequencing of a laccase gene from the lignin-degrading basidiomycete Pleurotus ostreatus

Cited by 125 publications

References 31 publications

The use of amplified flanking region-PCR in the isolation of laccase promoter sequences from the edible fungus Pleurotus sajor-caju

The use of amplified flanking region-PCR in the isolation of laccase promoter sequences from the edible fungus Pleurotus sajor-caju

Cloning of an acidic laccase gene (clac2) from Coprinus congregatus and its expression by external pH

Purification and characterization of a growth-regulating laccase from Pleurotus florida

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