Characterization of a cDNA encoding a manganese peroxidase, from the lignin-degrading basidiomycete Phanerochaete chrysosporium.

A cDNA clone of a manganese peroxidase (MnP) from Phanerochaete chrysosporium was isolated and characterized. The cDNA contains 1314 nucleotides excluding the poly(A) tail and the coding region has 68% G + C content. The deduced mature MnP protein contains 357 amino acids and is preceded by a 21-amino acid leader sequence. The experimentally determined N-terminal sequence of the purified MnP-1 protein, pI = 4.9, corresponds to the deduced N-terminal sequence of the gene. The Mr of the mature MnP-1 deduced from the cDNA is 37,439, which is approximately 81.4% of the experimentally determined molecular weight. The difference is due to glycosylation and a single potential N-glycosylation site with the general sequence Asn-X-Thr/Ser is present in the deduced MnP-1 sequence. Consistent with the peroxidase mechanism of MnP, the proximal histidine, the distal histidine, and the distal arginine are all conserved and regions flanking these residues display homology with other peroxidases. Northern blot analysis indicates that MnP expression is controlled by nutrient nitrogen at the level of transcription. Southern blot hybridization analysis suggests that MnP-1 is a member of a family of MnP genes.