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pubmed-article:16255241pubmed:abstractTextThe salicylic acid-induced protein kinase (SIPK) of tobacco, which is a mitogen-activated protein kinase (MAPK), is activated by various biotic and abiotic treatments. Overexpression of SIPK has been shown to trigger cell death. In this study, a targeted yeast two-hybrid approach identified the tobacco transcription factor WRKY1 as a potential substrate. SIPK phosphorylated WRKY1, which resulted in enhanced DNA-binding activity of WRKY1 to its cognate binding site, a W box sequence from the tobacco chitinase gene CHN50. SIPK-mediated enhancement of WRKY1 DNA-binding activity was inhibited by staurosporine, a general kinase inhibitor. Co-expression of SIPK and WRKY1 in Nicotiana benthamiana led to more rapid cell death than expression of SIPK alone, suggesting that WRKY1 is involved in the formation of hypersensitive response-like cell death and may be a component of the signaling cascade downstream of SIPK.lld:pubmed
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pubmed-article:16255241pubmed:pagination1027-34lld:pubmed
pubmed-article:16255241pubmed:dateRevised2009-11-19lld:pubmed
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pubmed-article:16255241pubmed:articleTitleTobacco transcription factor WRKY1 is phosphorylated by the MAP kinase SIPK and mediates HR-like cell death in tobacco.lld:pubmed
pubmed-article:16255241pubmed:affiliationBoyce Thompson Institute for Plant Research, Ithaca, NY 14853, USA.lld:pubmed
pubmed-article:16255241pubmed:publicationTypeJournal Articlelld:pubmed
pubmed-article:16255241pubmed:publicationTypeResearch Support, U.S. Gov't, Non-P.H.S.lld:pubmed
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