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Molecular Characterization of the Oxalate Oxidase Involved in the Response of Barley to the Powdery Mildew Fungus1

Fasong Zhou2, Ziguo Zhang2, 3, Per L. Gregersen, Jørn D. Mikkelsen, Eigil de Neergaard, David B. Collinge, and Hans Thordal-Christensen*

Plant Pathology Section, Department of Plant Biology, The Royal Veterinary and Agricultural University, Thorvaldsensvej 40, DK-1871 Frederiksberg C, Copenhagen, Denmark (F.Z., Z.Z., P.L.G., E.d.N., D.B.C., H.T.-C.); and Danisco Biotechnology, Copenhagen, Denmark (J.D.M.)

Previously we reported that oxalate oxidase activity increases in extracts of barley (Hordeum vulgare) leaves in response to the powdery mildew fungus (Blumeria [syn. Erysiphe] graminis f.sp. hordei) and proposed this as a source of H2O2 during plant-pathogen interactions. In this paper we show that the N terminus of the major pathogen-response oxalate oxidase has a high degree of sequence identity to previously characterized germin-like oxalate oxidases. Two cDNAs were isolated, pHvOxOa, which represents this major enzyme, and pHvOxOb', representing a closely related enzyme. Our data suggest the presence of only two oxalate oxidase genes in the barley genome, i.e. a gene encoding HvOxOa, which possibly exists in several copies, and a single-copy gene encoding HvOxOb. The use of 3' end gene-specific probes has allowed us to demonstrate that the HvOxOa transcript accumulates to 6 times the level of the HvOxOb transcript in response to the powdery mildew fungus. The transcripts were detected in both compatible and incompatible interactions with a similar accumulation pattern. The oxalate oxidase is found exclusively in the leaf mesophyll, where it is cell wall located. A model for a signal transduction pathway in which oxalate oxidase plays a central role is proposed for the regulation of the hypersensitive response.

1   This study was supported by the Danish Agricultural and Veterinary Research Council, by the Daloon Foundation, Denmark (F.Z.), and by the Carlsberg Foundation (H.T.-C.).
2   Permanent address: Department of Agronomy, Huazhong Agricultural University, Wuhan, People's Republic of China.
3   Present address: Department of Plant Sciences, University of Oxford, UK.
*   Corresponding author; e-mail htc{at}kvl.dk; fax 45-35-28- 33-10.

Plant Physiol. (1998) 117: 33-41
Copyright Clearance Center:   0032-0889/98/117/0033/09
© 1998 American Society of Plant Physiologists




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