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Protein Phosphorylation Is Induced in Tobacco Cells by the Elicitor Cryptogein

M. P. Viard, F. Martin, A. Pugin, P. Ricci, J. P. Blein
M. P. Viard
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F. Martin
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A. Pugin
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P. Ricci
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J. P. Blein
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Published April 1994. DOI: https://doi.org/10.1104/pp.104.4.1245

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Abstract

Changes in plasmalemma ion fluxes were observed when tobacco (Nicotiana tabacum) cells were treated with cryptogein, a proteinaceous elicitor from Phytophthora cryptogea. A strong alkalization of the culture medium, accompanied by a leakage of potassium, was induced within a few minutes of treatment. These effects reached a maximum after 30 to 40 min and lasted for several hours. This treatment also resulted in a rapid, but transient, production of activated oxygen species. All these physiological responses were fully sensitive to staurosporine, a known protein kinase inhibitor. Furthermore, a study of protein phosphorylation showed that cryptogein induced a staurosporine-sensitive phosphorylation of several polypeptides. These data suggest that phosphorylated proteins may be essential for the transduction of elicitor signals.

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Protein Phosphorylation Is Induced in Tobacco Cells by the Elicitor Cryptogein
M. P. Viard, F. Martin, A. Pugin, P. Ricci, J. P. Blein
Plant Physiology Apr 1994, 104 (4) 1245-1249; DOI: 10.1104/pp.104.4.1245

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Protein Phosphorylation Is Induced in Tobacco Cells by the Elicitor Cryptogein
M. P. Viard, F. Martin, A. Pugin, P. Ricci, J. P. Blein
Plant Physiology Apr 1994, 104 (4) 1245-1249; DOI: 10.1104/pp.104.4.1245
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Plant Physiology
Vol. 104, Issue 4
Apr 1994
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  • The Three-Dimensional Structure of Pectate Lyase E, a Plant Virulence Factor from Erwinia chrysanthemi
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