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High-affinity salicylic acid-binding protein 2 is required for plant innate immunity and has salicylic acid-stimulated lipase activity
Dhirendra Kumar
Daniel F. Klessig*
Boyce Thompson Institute for Plant Research, Tower Road, Ithaca, NY 14853
Received for publication October 12, 2003.
Abstract:
Salicylic acid (SA) is a critical hormone for signaling innateimmunity in plants. Here we present the purification and characterizationof SA-binding protein 2 (SABP2), a tobacco protein that is presentin low abundance and specifically binds SA with high affinity.Sequence analysis predicted that SABP2 is a lipase belongingto the α/β fold hydrolase super family. Confirmingthis prediction, recombinant SABP2 exhibited lipase activityagainst several synthetic substrates. Moreover, this lipaseactivity was stimulated by SA binding and may generate a lipid-derivedsignal. Silencing of SABP2 expression suppressed local resistanceto tobacco mosaic virus, induction of pathogenesis-related 1(PR-1) gene expression by SA, and development of systemic acquiredresistance. Together, these results suggest that SABP2 is anSA receptor that is required for the plant immune response.We further propose that SABP2 belongs to a large class of ligand-stimulatedhydrolases involved in stress hormone-mediated signal transduction.
* To whom correspondence should be addressed. E-mail: dfk8{at}cornell.edu.
Communicated by June B. Nasrallah, Cornell University, Ithaca,NY, November 4, 2003
Data deposition: The sequences reported in this paper have beendeposited in the GenBank database [accession nos. AY485932
[GenBank]
(SABP2);AAO22676
[GenBank]
(A. thaliana), CAA11219
[GenBank]
(M. esculenta), P52704
[GenBank]
(H.brasiliensis), and Q43360
[GenBank]
(O. sativa, Pir7b)].
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