Enhancement of minor laccases production in the basidiomycete Marasmius quercophilus C30

Klonowska, A

doi:10.1016/s0378-1097(01)00192-6

Cited by 21 publications

(40 citation statements)

References 14 publications

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“…The sequences of all MREs are similar to the core MRE consensus sequence (59-TGCRCNC-39) identified in metallothionein (mt) gene promoters (Thiele, 1992). Other laccase promoters have been reported to contain multiple putative MRE sites (Karahanian et al, 1998;Mansur et al, 1998;Galhaup et al, 2002;Klonowska et al, 2001). …”

Section: Introductionmentioning

confidence: 55%

Metal-responsive elements in Pleurotus ostreatus laccase gene promoters

2003

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Fungal laccase gene transcription is strongly induced by copper ions; notably, some laccase promoters contain multiple putative metal-responsive elements (MREs). Previously, it has been demonstrated that the Pleurotus ostreatus laccase genes poxc and poxa1b are transcriptionally induced by copper, and several putative MREs were found in the promoter regions of these genes, which extend for about 400 nt upstream of the start codon (ATG). Identification of MRE sequences, which are protected by protein binding in the poxc and poxa1b promoter regions, has been achieved by footprinting analyses. Electromobility shift assays led to the evaluation of the ability of the identified MREs to bind protein(s), and the role of specific nucleotides of these elements in complex formation has also been analysed. The formation of complexes between analysed MREs and fungal proteins requires the absence of metal ions. Proteins extracted from fungus grown in copper-depleted medium are able to form complexes with MREs, whilst proteins extracted from fungus grown in copper-containing medium are able to form complexes only in the presence of a metal chelator. Moreover, copper-depleted proteins are unable to form complexes when copper or zinc ions are added. UV-cross-linking analyses led to the determination of the molecular masses of the MRE-binding proteins. In the poxa1b promoter, a GC-rich region, homologous to the core binding site for transcription factor Sp1, decreases the binding affinity of the adjacent MRE, affecting its interactions with fungal protein factors.

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Section: Introductionmentioning

confidence: 55%

Metal-responsive elements in Pleurotus ostreatus laccase gene promoters

2003

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“…(0.05-1 mM) induced both Lac1 and Lac2. Copper is a strong inducer of laccase in many fungal species, including Trametes versicolor (L.) Lloyd (Collins and Dobson 1997), Marasmius quercophilus Pouzar (Klonowsk et al 2001), Pleurotus ostreatus (Jacq.) P. Kumm.…”

Section: Discussionmentioning

confidence: 99%

Effect of Cu2+, Mn2+ and aromatic compounds on the production of laccase isoforms by Coprinus comatus

Lu¹,

Ding²

2010

Mycoscience

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Six different extracellular laccase isoforms were identified in submerged cultures of the commercially important edible mushroom, Coprinus comatus. Although laccase activity (*55 IU/L) was readily detectable in unsupplemented control cultures containing 1.6 lM Cu 2? after 22-day incubation, mean enzyme levels (*150-185 IU/L) were 2.7-3.4-fold higher in cultures supplemented with 0.5-3.0 mM Cu 2? . Laccase production was also stimulated by Mn supplementation over the range 0.05-0.8 mM Mn 2? , and the peak value of *225 IU/L recorded after 22 days in cultures containing 0.8 mM added Mn 2? was 4.5-fold higher compared with unsupplemented controls. Of 12 aromatic compounds tested for their effect on laccase isozyme production by C. comatus, highest laccase levels (*188 IU/L), equivalent to a 4.4-fold increase compared with unsupplemented controls (*43 IU/L), were recorded after 22 days in cultures supplemented with 3.0 mM caffeic acid. Other aromatic compounds tested all stimulated laccase production, with peak enzyme levels 1.3-3.3-fold higher compared with unsupplemented controls. Extracellular laccase levels in cultures supplemented with optimal concentrations of Mn 2? and caffeic acid together were 38% and 15% lower, respectively, compared with cultures containing the separate supplements. Lac1 was the most abundant laccase isoform produced under all the conditions tested, but marked differences were observed in the production patterns of Lac2-Lac6.

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“…In response to inducers, laccase gene expression varies from fungus to fungus [23]. For example, Klonowska et al (2001) [55] showed that Marasmius quercophilus C30 produces at least four laccases. Production of two laccase forms by the fungus Volvariella volvacea was shown during induction by ferulic acid, 4-hydroxybenzoic acid, р-hydroxybenzaldehyde, veratryl acid, CuSO 4 , and xylidine [56].…”

Section: Discussionmentioning

confidence: 99%

Influence of PAHs on ligninolytic enzymes of the fungus Pleurotus ostreatus D1

2010

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Polycyclic aromatic hydrocarbons (PAHs), their derivatives, and their degradation products were assayed for the ability to enhance activities of ligninolytic enzymes (laccase and versatile peroxidase) of the fungus Pleurotus ostreatus D1. The activities of both laccase and versatile peroxidase were induced by the PAHs, their derivatives, and their degradation products. Laccase was produced mostly in the first 7-10 days, whereas the production of versatile peroxidase began after 5-7 days of cultivation. Non-denaturing PAGE showed the presence of additional forms of laccase and versatile peroxidase in the presence of the xenobiotics in the cultivation medium. The difference in the production time for these enzymes may reflect that laccases are involved in the first stages of PAHs degradation and that versatile peroxidase can be necessary for oxidation of some degradation products. This is the first report on versatile peroxidase induction by PAHs and their derivatives.

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Enhancement of minor laccases production in the basidiomycete Marasmius quercophilus C30

Cited by 21 publications

References 14 publications

Metal-responsive elements in Pleurotus ostreatus laccase gene promoters

Metal-responsive elements in Pleurotus ostreatus laccase gene promoters

Effect of Cu2+, Mn2+ and aromatic compounds on the production of laccase isoforms by Coprinus comatus

Influence of PAHs on ligninolytic enzymes of the fungus Pleurotus ostreatus D1

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