A hitherto undescribed black yeast was isolated from an extract of brown coal containing humic and fulvic acids at pH 0.6. The fungus showed morphological similarity to some members of the genus Exophiala (Chaetothyriales) and of Hortaea (Dothideales). Based on SSU rDNA sequence similarity to meristematic members of the Dothideales, the new species was accommodated in Hortaea, which presently contains only a single, halophilic species, H. werneckii.

The expression of glutamic acid decarboxylase gene and the laccase activity were measured during the development of surface-cultivated Trichoderma viride mycelia in order to examine their up-regulation by light. The results show that the changes in activity of GAD induced by light observed previously are caused by transcriptional regulation of gad gene expression in both submerged mycelia and aerial mycelia after photoinduction. The expression of tga gene encoding a T. viride G(alpha) protein was found not to be up-regulated by light and was also present in the non-conidiating mutant of T. viride suggesting that this protein is not involved in the regulation of conidiation in this fungus, or that it plays a role is in later stages of conidia development. The activity of laccase was also not light-inducible and may be related to the maturation of conidia.

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The pigmented ascomycete Hortaea acidophila is able to grow at a pH as low as 0.6 and produces laccases that are involved in melanin synthesis. We now present data on an extracellular and an intracellular laccase which exhibit a high stability at low pH. Furthermore, the optimum for enzyme acitivity is extraordinarily low with pH 1.5 for the intracellular laccase with 2,6-dimethoxyphenol (DMOP) as substrate. Two complete laccase gene sequences of H. acidophila were amplified by inverse polymerase chain reaction (PCR). Whereas the deduced protein laccase I contains an predicted N-terminal signal sequence for protein export, laccase II does not and thus may represent the intracellular laccase. The acidophilic character of both laccases seems to be reflected in their primary structure.

Hortaea acidophila is a pigmented, yeast-like ascomycete that is able to grow at a pH as low as 0.6. This study presents evidence that H. acidophila possesses at least two functional laccases that seem to be involved in melanin synthesis. This evidence is supported by PCR amplification of laccase-specific gene fragments by using primers derived from conserved copper-binding-regions and by Southern Blot analysis. Due to their low pH optimum the laccases may be of special interest for biotechnological use.