October
2005
, Volume
18
, Number
10
Pages
1,027
-
1,034
Authors
Frank L. H.
Menke
,
1
Hong-Gu
Kang
,
1
Zhixiang
Chen
,
2
Jeong Mee
Park
,
1
Dhirendra
Kumar
,
1
and
Daniel F.
Klessig
1
Affiliations
1Boyce Thompson Institute for Plant Research, Tower Road, Ithaca, NY 14853, U.S.A.; and 2Department of Botany and Plant Pathology, Purdue University, 915 West State Street, West Lafayette, IN 47907, U.S.A.
Go to article:
RelatedArticle
Accepted 16 June 2005.
Abstract
The 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.
JnArticleKeywords
Page Content
ArticleCopyright
© 2005 The American Phytopathological Society