Structures of genomic and complementary DNAs coding for Pleurotus ostreatus manganese (II) peroxidase.
To study the mechanism of regulation and structure/function relationship of the Pleurotus ostreatus manganese (II) peroxidase (MnP), we amplified the full-length genomic and complementary DNAs for the major isozyme of the MnP mainly by the cassette-primer PCR technique and then sequenced them. The cDNA contained an open reading frame of 1083 bp encoding for a polypeptide of 361 amino-acid residues, including the suggested signal peptide of 29 amino-acid residues with a prepro structure. The predicted amino-acid sequence of the protein shared several common characteristics with those of fungal lignin and manganese (II) peroxidases. We could find a suggested metal response element and two heat-shock element-like sequences in the 5'-flanking region of the structural gene. The structural gene contained 15 introns, many of which lie identical to those in lignin peroxidase genes rather than to those in the known MnP genes.
Asada
Y
Y
Department of Bioresource Science, Faculty of Agriculture, Kagawa University, Japan.
Watanabe
A
A
Irie
T
T
Nakayama
T
T
Kuwahara
M
M
D000595:Amino Acid Sequence; D001483:Base Sequence; D018076:DNA, Complementary / Q000737:chemistry*; D008969:Molecular Sequence Data; D010544:Peroxidases / Q000235:genetics*; D011124:Polyporaceae / Q000201:enzymology* / Q000235:genetics; D016415:Sequence Alignment
D018076:DNA, Complementary; D010544:Peroxidases; C051129:manganese peroxidase