Phylogenetic analysis, genomic organization, and expression analysis of multi-copper oxidases in the ectomycorrhizal basidiomycete Laccaria bicolor.
In forest soils, ectomycorrhizal and saprotrophic Agaricales differ in their strategies for carbon acquisition, but share common gene families encoding multi-copper oxidases (MCOs). These enzymes are involved in the oxidation of a variety of soil organic compounds. The MCO gene family of the ectomycorrhizal fungus Laccaria bicolor is composed of 11 genes divided into two distinct subfamilies corresponding to laccases (lcc) sensu stricto (lcc1 to lcc9), sharing a high sequence homology with the coprophilic Coprinopsis cinerea laccase genes, and to ferroxidases (lcc10 and lcc11) that are not present in C. cinerea. The fet3-like ferroxidase genes lcc10 and lcc11 in L. bicolor are each arranged in a mirrored tandem orientation with an ftr gene coding for an iron permease. Unlike C. cinerea, L. bicolor has no sid1/sidA gene for siderophore biosynthesis. Transcript profiling using whole-genome expression arrays and quantitative reverse transcriptase-polymerase chain reaction (qRT-PCR) revealed that some transcripts were very abundant in ectomycorrhizas (lcc3 and lcc8), in fruiting bodies (lcc7) or in the free-living mycelium grown on agar medium (lcc9 and lcc10), suggesting a specific function of these MCOs. The amino acid composition of the MCO substrate binding sites suggests that L. bicolor MCOs interact with substrates different from those of saprotrophic fungi.
Courty
P E
PE
UMR 1136 INRA-Nancy Université, Interactions Arbres/Microorganisms, INRA-Nancy, 54280 Champenoux, France.|Botanical Institute, University of Basel, CH-4056 Basel, Switzerland.
Hoegger
P J
PJ
Molecular Wood Biotechnology and Technical Mycology, Büsgen-Institute, Georg-August-University, D-37077 Göttingen, Germany.
Kilaru
S
S
Molecular Wood Biotechnology and Technical Mycology, Büsgen-Institute, Georg-August-University, D-37077 Göttingen, Germany.
Kohler
A
A
UMR 1136 INRA-Nancy Université, Interactions Arbres/Microorganisms, INRA-Nancy, 54280 Champenoux, France.
Buée
M
M
UMR 1136 INRA-Nancy Université, Interactions Arbres/Microorganisms, INRA-Nancy, 54280 Champenoux, France.
Garbaye
J
J
UMR 1136 INRA-Nancy Université, Interactions Arbres/Microorganisms, INRA-Nancy, 54280 Champenoux, France.
Martin
F
F
UMR 1136 INRA-Nancy Université, Interactions Arbres/Microorganisms, INRA-Nancy, 54280 Champenoux, France.
Kües
U
U
Molecular Wood Biotechnology and Technical Mycology, Büsgen-Institute, Georg-August-University, D-37077 Göttingen, Germany.
D000595:Amino Acid Sequence; D002570:Ceruloplasmin / Q000235:genetics; D005656:Fungal Proteins / Q000235:genetics / Q000378:metabolism; D015966:Gene Expression Regulation, Fungal; D016681:Genome, Fungal / Q000235:genetics*; D007438:Introns / Q000235:genetics; D055399:Laccaria / Q000201:enzymology* / Q000235:genetics*; D042845:Laccase / Q000737:chemistry / Q000235:genetics / Q000378:metabolism; D008969:Molecular Sequence Data; D038821:Mycorrhizae / Q000201:enzymology / Q000235:genetics*; D010088:Oxidoreductases / Q000235:genetics* / Q000378:metabolism; D010802:Phylogeny; D012045:Regulatory Sequences, Nucleic Acid; D020133:Reverse Transcriptase Polymerase Chain Reaction; D016415:Sequence Alignment
D005656:Fungal Proteins; D010088:Oxidoreductases; D042845:Laccase; C024748:copper oxidase; D002570:Ceruloplasmin