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Slow and Prolonged Activation of the p47 Protein Kinase during
Hypersensitive Cell Death in a Culture of
Tobacco Cells
Kaoru Suzuki*,
Akira Yano1, and
Hideaki Shinshi
Plant Molecular Biology Laboratory, National Institute of
Bioscience and Human Technology, Agency of Industrial Science and
Technology, Ministry of International Trade and Industry, 1-1
Higashi, Tsukuba, Ibaraki 305-8566, Japan
To investigate the involvement of
protein kinases in the signaling cascade that leads to hypersensitive
cell death, we used a previously established system in which a fungal
elicitor, xylanase from Trichoderma viride (TvX),
induces a hypersensitive reaction in tobacco (Nicotiana
tabacum) cells in culture (line XD6S). The elicitor induced the
slow and prolonged activation of a p47 protein kinase, which has the
characteristics of a family member of the mitogen-activated protein
kinases. An inhibitor of protein kinases, staurosporine, and a blocker
of Ca channels, Gd3+ ions, both of which blocked the
TvX-induced hypersensitive cell death, inhibited the TvX-induced
activation of p47 protein kinase. Moreover, an inhibitor of
serine/threonine protein phosphatase alone induced both rapid cell
death and the persistent activation of the p47 protein kinase. Thus,
the p47 protein kinase might be a component of the signal transduction
pathway that leads to hypersensitive cell death, and the regulation of
the duration of activation of the p47 protein kinase might be important
in determining the destiny of tobacco cells.
1
Present address: Department of Oral Science,
National Institute of Infectious Diseases, 1-23-1 Toyama,
Shinjuku-ku, Tokyo 162-8640, Japan.
*
Corresponding author; e-mail: skaoru{at}nibh.go.jp; fax:
81-298-54-6090.
Plant Physiol. (1999) 119: 1465-1472
Copyright Clearance Center: 0032-0889/99/119//08
© 1999 American Society of Plant Physiologists
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