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Plant Immunity Requires Conformational Charges of NPR1 via S-Nitrosylation and Thioredoxins

NPR1 is regulated by the opposing action of S-nitrosoglutathione and thioredoxins, as Yasuomi Tada and colleagues from the Duke University (USA) report.
Changes in redox status during could be observed in several different organisms. In , the conformation of NPR1 is regulated by those redox changes. NPR1 is a master regulator of salicylic acid–mediated genes that control . NPR1 is sequestered in the cytoplasm as an oligomer through intermolecular disulfide bonds.

NPR1 is S-nitrosylated by S-nitrosoglutathione at cysteine-156. This reaction enhances its oligomerisation, which is important to maintain protein homeostasis when salicylic acid is added. The NPR1 oligomer-to-monomer reaction, triggered by salicylic acid, is catalysed by thioredoxins. NPR1 reliant disease resistance was impaired by mutations in NPR1 cysteine-156 as well as thioredoxins. It seems, pathogen-triggered redox changes and gene regulation are important to .

Related antibodies on antibodies-online.com:

NPR1

Salicylic acid (acetylated)

Thioredoxin (Trx) Family Antibody Sampler Kit

Antibodies for the research area immunology:

Antibodies for the research area plant physiology:

Antibodies for the research area signalling: