Primary structure and transcription analysis of a laccase-encoding gene from the basidiomycete Trametes trogii

Colao, M. Ch.; Garzillo, Anna Maria Vittoria; Buonocore, Vincenzo; Schiesser, A.; Ruzzi, Maurizio

doi:10.1007/s00253-003-1429-x

Cited by 33 publications

(23 citation statements)

References 23 publications

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“…Laccase induction at the transcriptional level has been reported to occur under nonlimiting nitrogen levels in T. versicolor [4] and in the ligninolytic basidiomycete I62 [167]. Expression of lcc1 in T. trogii is preferentially induced by organic nitrogen sources compared with inorganic ones [168]. Individual laccase isoenzyme genes in P. sajor-caju are differentially induced at the transcriptional level by nitrogen sources.…”

Section: Aromatic Compoundsmentioning

confidence: 99%

Laccases: a never-ending story

Giardina¹,

Faraco²,

Pezzella³

et al. 2009

Cell. Mol. Life Sci.

866

638

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Laccases (benzenediol:oxygen oxidoreductases, EC 1.10.3.2) are blue multicopper oxidases that catalyze the oxidation of an array of aromatic substrates concomitantly with the reduction of molecular oxygen to water. In fungi, laccases carry out a variety of physiological roles during their life cycle. These enzymes are being increasingly evaluated for a variety of biotechnological applications due to their broad substrate range. In this review, the most recent studies on laccase structural features and catalytic mechanisms along with analyses of their expression are reported and examined with the aim of contributing to the discussion on their structure-function relationships. Attention has also been paid to the properties of enzymes endowed with unique characteristics and to fungal laccase multigene families and their organization.

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Section: Aromatic Compoundsmentioning

confidence: 99%

Laccases: a never-ending story

Giardina¹,

Faraco²,

Pezzella³

et al. 2009

Cell. Mol. Life Sci.

866

638

View full text Add to dashboard Cite

show abstract

“…Expression of lcc1 in Tramtes trogii is preferentially induced by organic nitrogen sources compared with inorganic ones [59]. Individual laccase genes in P. sajor-caju are differentially induced at the transcriptional level by nitrogen sources, with a positive regulation by nitrogen occurring for lac2 and lac4 , and no effect being detected for lac1 and lac3 [8].…”

Section: Laccase Inductionmentioning

confidence: 99%

Induction and Transcriptional Regulation of Laccases in Fungi

Piscitelli

Giardina²,

Lettera³

et al. 2011

285

219

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Fungal laccases are phenol oxidases widely studied for their use in several industrial applications, including pulp bleaching in paper industry, dye decolourisation, detoxification of environmental pollutants and revalorization of wastes and wastewaters. The main difficulty in using these enzymes at industrial scale ensues from their production costs. Elucidation of the components and the mechanisms involved in regulation of laccase gene expression is crucial for increasing the productivity of native laccases in fungi. Laccase gene transcription is regulated by metal ions, various aromatic compounds related to lignin or lignin derivatives, nitrogen and carbon sources. In this manuscript, most of the published results on fungal laccase induction, as well as analyses of both the sequences and putative functions of laccase gene promoters are reviewed. Analyses of promoter sequences allow defining a correlation between the observed regulatory effects on laccase gene transcription and the presence of specific responsive elements, and postulating, in some cases, a mechanism for their functioning. Only few reports have investigated the molecular mechanisms underlying laccase regulation by different stimuli. The reported analyses suggest the existence of a complex picture of laccase regulation phenomena acting through a variety of cis acting elements. However, the general mechanisms for laccase transcriptional regulation are far from being unravelled yet.

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“…The bacterial lacZ gene was excised from plasmids pMD12 (5) and pMD12RR (5) by HindIII digestion and replaced with a HindIII fragment containing the cDNA of the laccase gene lcc1 from the fungus Trametes trogii (4). The plasmid harboring the lcc1 cDNA was a kind gift of M. Ruzzi.…”

Section: Methodsmentioning

confidence: 99%

Induction by Hypoxia of Heterologous-Protein Production with the Kl PDC1 Promoter in Yeasts

Camattari

Bianchi

Branduardi

et al. 2007

Appl Environ Microbiol

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The control of promoter activity by oxygen availability appears to be an intriguing system for heterologous protein production. In fact, during cell growth in a bioreactor, an oxygen shortage is easily obtained simply by interrupting the air supply. The purpose of our work was to explore the possible use of hypoxic induction of the KlPDC1 promoter to direct heterologous gene expression in yeast. In the present study, an expression system based on the KlPDC1 promoter was developed and characterized. Several heterologous proteins, differing in size, origin, localization, and posttranslational modification, were successfully expressed in Kluyveromyces lactis under the control of the wild type or a modified promoter sequence, with a production ratio between 4 and more than 100. Yields were further optimized by a more accurate control of hypoxic physiological conditions. Production of as high as 180 mg/liter of human interleukin-1␤ was obtained, representing the highest value obtained with yeasts in a lab-scale bioreactor to date. Moreover, the transferability of our system to related yeasts was assessed. The lacZ gene from Escherichia coli was cloned downstream of the KlPDC1 promoter in order to get ␤-galactosidase activity in response to induction of the promoter. A centromeric vector harboring this expression cassette was introduced in Saccharomyces cerevisiae and in Zygosaccharomyces bailii, and effects of hypoxic induction were measured and compared to those already observed in K. lactis cells. Interestingly, we found that the induction still worked in Z. bailii; thus, this promotor constitutes a possible inducible system for this new nonconventional host.

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Primary structure and transcription analysis of a laccase-encoding gene from the basidiomycete Trametes trogii

Cited by 33 publications

References 23 publications

Laccases: a never-ending story

Laccases: a never-ending story

Induction and Transcriptional Regulation of Laccases in Fungi

Induction by Hypoxia of Heterologous-Protein Production with the Kl PDC1 Promoter in Yeasts

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