4/28/2024 0 Comments Tree branch toca block![]() ![]() ![]() It was established that all Basidiomycete laccases form a single monophyletic branch – sensu stricto laccases – and many of them occasionally occur on tree leaves, according to the taxonomical associations of the corresponding fungal species ( Hoegger et al., 2006 Kües and Rühl, 2011), suggesting both the absence of extensive gene conversion and a relatively small number of species-specific duplications. Moreover, all present works are very broad in their sampled taxa, incomplete in their inclusion of entire laccase multigene families and, consequently, are highly general in their conclusions. It would be fair to say that, although many different laccase phylogenetic trees have been constructed with different purposes throughout the literature, at the moment, there is only a small number of works directly devoted to the evolution of laccases ( Valderrama et al., 2003 Hoegger et al., 2006 Billette et al., 2011 Kües and Rühl, 2011). It is currently well established that fungal genomes almost always contain several non-allelic copies of sensu stricto laccase-encoding genes – known as laccase multigene families nevertheless, many aspects of evolution and functions of these families remain unknown. Broad substrate specificity and high stability make laccase a prospective enzyme for different biotechnological applications ( Riva, 2006 Rodríguez Couto and Toca Herrera, 2006 Mate and Alcalde, 2017). Laccases (benzene diol:dioxygen oxidoreductases EC 1.10.3.2 CAZy – AA1_1) are blue MCOs that catalyze single-electron abstractions from various phenolic and non-phenolic compounds, with a concomitant reduction of molecular oxygen to water ( Baldrian, 2006 Morozova et al., 2007 Giardina et al., 2010 Mogharabi and Faramarzi, 2014). Oddly enough, there are no recent reports devoted specifically to the evolution of laccases, which, along with peroxidases, are the main components of the extracellular enzymatic complex of white rot fungi. Moreover, sequences of several ancestral peroxidase genes were inferred, and the corresponding enzymes were heterologously expressed and biochemically characterized ( Semba et al., 2015 Ayuso-Fernández et al., 2017, 2018). Evolution of these enzymes was traced back to the Carboniferous geological period and associated with an appearance of different wood-decay strategies (i.e., white rot and brown rot) later in the Cretaceous ( Floudas et al., 2012 Ruiz-Dueñas et al., 2013 Krah et al., 2018). This notorious progress has been achieved in the case of fungal class II peroxidases (i.e., manganese, lignin and versatile peroxidases). In the last decade, there has been an increasing interest in the evolution of wood-degrading fungi in general and their ligninolytic enzyme complex in particular ( Binder et al., 2013 Riley et al., 2014 Justo et al., 2017). Moreover, their ability to efficiently degrade lignocellulose biomass makes wood-rotting fungi, especially white rot fungi from the order Polyporales (Basidiomycota, Fungi), an attractive target for many biotechnological applications, such as the production of biofuel, biopulping and bioremediation ( Pérez et al., 2002 Hatakka and Hammel, 2011 Fisher and Fong, 2014). In addition to their fundamental roles in carbon balance, soil formation and forest regeneration, wood-rotting fungi provide a habitat for various organisms that support the biodiversity of our planet ( Jönsson et al., 2008 Lonsdale et al., 2008 Marcot, 2017). Wood-rotting fungi are crucial components of many terrestrial ecosystems. In addition, we provide a comparison of the biochemical and catalytic properties of the four laccase isozymes from Trametes hirsuta and suggest their functional diversification within the multigene family. The conducted analysis provides a better understanding of the Polyporales laccase multigenicity and allows for the systemization of the individual features of different laccase isozymes. Here, we present a detailed evolutionary analysis of the sensu stricto laccase genes (CAZy – AA1_1) from fungi of the Polyporales order. It is currently well established that fungal genomes almost always contain several non-allelic copies of laccase genes (laccase multigene families) nevertheless, many aspects of laccase multigenicity, for example, their precise biological functions or evolutionary relationships, are mostly unknown. ![]() Laccase is one of the oldest known and intensively studied fungal enzymes capable of oxidizing recalcitrant lignin-resembling phenolic compounds. Bach Institute of Biochemistry, Research Center of Biotechnology, Russian Academy of Sciences, Moscow, Russia 2Laboratory of Gene Expression Optimization, A. ![]() 1Laboratory of Molecular Aspects of Biotransformations, A. ![]()
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