Abstract

A cDNA clone, lambda LPO-1, encoding a major lignin peroxidase from the basidiomycete Bjerkandera adusta was isolated and characterized. The nucleotide sequence of lambda LPO-1 predicts a mature protein consisting of 349 amino acids with a molecular weight of 37,225 preceded by a signal peptide of 23 amino acid residues. We have also cloned and sequenced the gene encoding lignin peroxidase from B. adusta. Comparison of these sequences reveals a lignin peroxidase gene structure consisting of 1,116 bp of protein-encoding DNA that is interrupted by four intervening sequences. The putative eukaryotic regulatory sequence, a TATA box, is present at position -75 relative to the translational initiation codon. Amino acid sequence homology between the coding regions of lambda LPO-1 and of the lignin peroxidase cDNA clone lambda ML-1 from Phanerochaete chrysosporium is 61%.

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