High-affinity salicylic acid-binding protein 2 is required for plant innate immunity and has salicylic acid-stimulated lipase activity

被引：216
作者：
Kumar, D [1 ]
Klessig, DF [1 ]
机构：
[1] Boyce Thompson Inst Plant Res, Ithaca, NY 14853 USA
来源：
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA | 2003年 / 100卷 / 26期
关键词：
D O I：
10.1073/pnas.0307162100
中图分类号：
O [数理科学和化学]; P [天文学、地球科学]; Q [生物科学]; N [自然科学总论];
学科分类号：
07 ; 0710 ; 09 ;
摘要：
Salicylic acid (SA) is a critical hormone for signaling innate immunity in plants. Here we present the purification and characterization of SA-binding protein 2 (SABP2), a tobacco protein that is present in low abundance and specifically binds SA with high affinity. Sequence analysis predicted that SABP2 is a lipase belonging to the alpha/beta fold hydrolase super family. Confirming this prediction, recombinant SABP2 exhibited lipase activity against several synthetic substrates. Moreover, this lipase activity was stimulated by SA binding and may generate a lipid-derived signal. Silencing of SABP2 expression suppressed local resistance to tobacco mosaic virus, induction of pathogenesis-related 1 (PR-1) gene expression by SA, and development of systemic acquired resistance. Together, these results suggest that SABP2 is an SA receptor that is required for the plant immune response. We further propose that SABP2 belongs to a large class of ligand-stimulated hydrolases involved in stress hormone-mediated signal transduction.
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页码：16101 / 16106
页数：6
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