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Nuclear Localization of NPR1 Is Required for Activation of PR Gene Expression
Author(s) -
Mark Kinkema,
Weihua Fan,
Xinnian Dong
Publication year - 2000
Publication title -
the plant cell
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 5.324
H-Index - 341
eISSN - 1532-298X
pISSN - 1040-4651
DOI - 10.1105/tpc.12.12.2339
Subject(s) - npr1 , biology , systemic acquired resistance , nuclear localization sequence , subcellular localization , signal transduction , fusion protein , microbiology and biotechnology , nuclear export signal , fusion gene , gene , natriuretic peptide , cell nucleus , genetics , nucleus , cytoplasm , heart failure , medicine , recombinant dna , arabidopsis , mutant
Systemic acquired resistance (SAR) is a broad-spectrum resistance in plants that involves the upregulation of a battery of pathogenesis-related (PR) genes. NPR1 is a key regulator in the signal transduction pathway that leads to SAR. Mutations in NPR1 result in a failure to induce PR genes in systemic tissues and a heightened susceptibility to pathogen infection, whereas overexpression of the NPR1 protein leads to increased induction of the PR genes and enhanced disease resistance. We analyzed the subcellular localization of NPR1 to gain insight into the mechanism by which this protein regulates SAR. An NPR1-green fluorescent protein fusion protein, which functions the same as the endogenous NPR1 protein, was shown to accumulate in the nucleus in response to activators of SAR. To control the nuclear transport of NPR1, we made a fusion of NPR1 with the glucocorticoid receptor hormone binding domain. Using this steroid-inducible system, we clearly demonstrate that nuclear localization of NPR1 is essential for its activity in inducing PR genes.

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