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Molecular and biochemical evidence for manganese-dependent peroxidase activity in Tylospora fibrillosa

Published online by Cambridge University Press:  01 September 1999

S. M. CHAMBERS
Affiliation:
Mycorrhiza Research Group, School of Science, University of Western Sydney (Nepean), PO Box 10, Kingswood, NSW 2747, Australia
R. M. BURKE
Affiliation:
Department of Biomolecular Science, UMIST, PO Box 88, Manchester, M60 1QD, U.K.
P. R. BROOKS
Affiliation:
Moredun Research Institute, 408 Gilmerton Rd, Edinburgh, EH17 7JH, U.K.
J. W. G. CAIRNEY
Affiliation:
Mycorrhiza Research Group, School of Science, University of Western Sydney (Nepean), PO Box 10, Kingswood, NSW 2747, Australia
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Abstract

Gel-based and spectrophotometric assays were used to demonstrate expression of a manganese-dependent peroxidase (MnP) activity in culture filtrates of the ectomycorrhizal basidiomycete Tylospora fibrillosa. PCR amplification using a primer pair specific for a 260 bp fragment from the 5′-end of a gene encoding an H3-like MnP isozyme in Phanerochaete chrysosporium, produced single amplification products of 260 bp from DNA extracted from two isolates of T. fibrillosa. The amplified fragment from T. fibrillosa had a 93·7% nucleotide overlap (over 201 bases) with a published sequence for a 260 base amplification product from the P. chrysosporium H3 MnP isozyme gene, strongly suggesting the presence of a homologous gene in the ectomycorrhizal fungus. The results are discussed in the context of lignin degradation by ectomycorrhizal fungi.

Type
Research Article
Copyright
© The British Mycological Society 1999

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