PMID: 9652390Jul 4, 1998Paper

The defense-related rice gene Pir7b encodes an alpha/beta hydrolase fold protein exhibiting esterase activity towards naphthol AS-esters

European Journal of Biochemistry
U WäspiR Dudler

Abstract

Acquired resistance of rice to Pyricularia oryzae, the causing agent of rice blast, can be induced by inoculation with the non-host pathogen Pseudomonas syringae pv. syringae. We have previously cloned a cDNA and a corresponding gene (Pir7b) whose transcripts accumulate upon infiltration with the resistance-inducing bacteria. The putative encoded product Pir7b exhibits significant sequence similarity to two recently cloned hydroxynitrile lyases from Manihot esculenta (cassava) and Hevea brasisliensis, enzymes involved in the release of hydrogen cyanide from cyanogenic glycosides. As rice does not contain cyanogenic glycosides, a similar function of Pir7b appears unplausible. In order to functionally characterize the protein, recombinant Pir7b was produced in Escherichia coli and Saccharomyces cerevisiae. We show that recombinant Pir7b does not have hydroxynitrile lyase activity, but exhibits esterase activity towards naphthol AS-acetate. Using Pir7b-specific antibodies, we show that the protein accumulates in rice leaves inoculated with P. syringae pv. syringae. Both the recombinant and the authentic proteins have an apparent molecular mass of 32 kDa (28.8 kDa calculated) and seem to be active as monomers. Pir7b esterase also e...Continue Reading

Citations

Apr 13, 2007·Molecular Genetics and Genomics : MGG·Takashi HikageKen-Ichi Tsutsumi
Jul 16, 2009·Plant Molecular Biology·Zhenyu GaoBin Han
May 10, 2000·Trends in Biotechnology·H GrienglM Fechter
Aug 3, 2012·Molecular Plant-microbe Interactions : MPMI·Christina RamelRobert Dudler
Jun 4, 2013·Annual Review of Phytopathology·Robert Dudler
Jul 20, 2007·The Plant Journal : for Cell and Molecular Biology·Shanfa LuVincent L Chiang
May 24, 2007·The Journal of Biological Chemistry·Markus C GershaterRobert Edwards

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