The Arabidopsis oligopeptidases TOP1 and TOP2 are salicylic acid targets that modulate SA-mediated signaling and the immune response

Moreau, M., Westlake, T., Zampogna, G., Popescu, G., Tian, M., Noutsos, C., Popescu, S. (November 2013) The Arabidopsis oligopeptidases TOP1 and TOP2 are salicylic acid targets that modulate SA-mediated signaling and the immune response. Plant Journal, 76 (4). pp. 603-614. ISSN 09607412

URL: http://www.ncbi.nlm.nih.gov/pubmed/24004003
DOI: 10.1111/tpj.12320

Abstract

Salicylic acid (SA) is a small phenolic molecule with hormonal properties, and is an essential component of the immune response. SA exerts its functions by interacting with protein targets; however, the specific cellular components modulated by SA and critical for immune signal transduction are largely unknown. To uncover cellular activities targeted by SA, we probed Arabidopsis protein microarrays with a functional analog of SA. We demonstrate that thimet oligopeptidases (TOPs) constitute a class of SA-binding enzymes. Biochemical evidence demonstrated that SA interacts with TOPs and inhibits their peptidase activities to various degrees both in vitro and in plant extracts. Functional characterization of mutants with altered TOP expression indicated that TOP1 and TOP2 mediate SA-dependent signaling and are necessary for the immune response to avirulent pathogens. Our results support a model whereby TOP1 and TOP2 act in separate pathways to modulate SA-mediated cellular processes.

Item Type: Paper
Subjects: organism description > plant > Arabidopsis
organs, tissues, organelles, cell types and functions > cell types and functions > cell functions
organs, tissues, organelles, cell types and functions > cell types and functions > cell functions > cell signaling
organs, tissues, organelles, cell types and functions > cell types and functions
organism description > plant
CSHL Authors:
Communities: CSHL labs > Ware lab
Depositing User: Matt Covey
Date: November 2013
Date Deposited: 11 Nov 2013 21:20
Last Modified: 23 Dec 2014 21:56
Related URLs:
URI: http://repository.cshl.edu/id/eprint/28860

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