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A new subfamily of fungal subtilases: structural and functional analysis of a Pleurotus ostreatus member

¹ Dipartimento di Chimica Organica e Biochimica, Università di Napoli ‘Federico II’, Complesso Universitario Monte S. Angelo, via Cinthia, 80126 Napoli, Italy
² ISPAAM, Consiglio Nazionale delle Ricerche, via Argine 1085, 80147 Napoli, Italy

Correspondence
Paola Giardina
giardina{at}unina.it

Pleurotus ostreatus produces several extracellular proteases which are believed to be involved in the regulation of the ligninolytic activities of this fungus. Recently, purification and characterization of the most abundant P. ostreatus extracellular protease (PoSl) have been reported. The sequence of the posl gene and of the corresponding cDNA has been determined, allowing the identification of its pre- and pro-sequences. A mature protein sequence has been verified by mass spectrometry mapping, the N-glycosylation sites have been identified and the glycosidic moieties characterized. Mature PoSl shows a cleaved peptide bond in the C-terminal region, which remains associated with the catalytic domain in a non-covalent complex. Reported results indicate that this enzyme is involved in the activation of other P. ostreatus secreted proteases, thus suggesting its leading role in cascade activation mechanisms. Analyses of the PoSl sequence by homology search resulted in the identification of a DNA sequence encoding a new protease, homologous to PoSl, in the Phanerochaete chrysosporium genome. A new subgroup of subtilisin-like proteases, belonging to the pyrolysin family, has been defined, which includes proteases from ascomycete and basidiomycete fungi.

The EMBL accession numbers for the nucleotide sequences reported in this paper are AJ634913 (posl) and AJ748587 (pcsl).