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Cited by 863

The DOI matches its Crossref record; 5 of the 5 references it cites were found in a registry or an index.

The Arabidopsis NPR1 Protein Is a Receptor for the Plant Defense Hormone Salicylic Acid

Open access
Wu, Yue, Zhang, Di, Chu, Jee Yan, Boyle, Patrick, Wang, Yong, Brindle, Ian D., De Luca, Vincenzo, Després, Charles·2012·Cell Reports

Abstract

Salicylic acid (SA) is an essential hormone in plant immunity, but its receptor has remained elusive for decades. The transcriptional coregulator NPR1 is central to the activation of SA-dependent defense genes, and we previously found that Cys(521) and Cys(529) of Arabidopsis NPR1's transactivation domain are critical for coactivator function. Here, we demonstrate that NPR1 directly binds SA, but not inactive structural analogs, with an affinity similar to that of other hormone-receptor interactions and consistent with in vivo Arabidopsis SA concentrations. Binding of SA occurs through Cys(521/529) via the transition metal copper. Mechanistically, our results suggest that binding of SA causes a conformational change in NPR1 that is accompanied by the release of the C-terminal transactivation domain from the N-terminal autoinhibitory BTB/POZ domain. While NPR1 is already known as a link between the SA signaling molecule and defense-gene activation, we now show that NPR1 is the receptor for SA.

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Crossref · 10.1016/j.celrep.2012.05.008

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Metadata

Authors
Wu, Y., Zhang, D., Chu, J. Y., Boyle, P., Wang, Y., Brindle, I. D., De Luca, V., & Després, C.
Venue
Cell Reports
Publisher
Elsevier BV
Published
2012-06
Volume
1
Issue
6
Pages
639-647
ISSN
2211-1247 (ISSN-L)
OpenAlex
W2156301059
Cited by
863
References
5
FWCI
57.37
Type
journal article
Language
en
Open access
gold

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Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).

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