Rapid and transient activation of a myelin basic protein kinase in tobacco leaves treated with harpin from Erwinia amylovora

Attila L. Ádám, Sharon Pike, M. Elizabeth Hoyos, Julie M. Stone, John C. Walker, Anton Novacky

Research output: Contribution to journalArticle

76 Citations (Scopus)

Abstract

Harpins are bacterial protein elicitors that induce hypersensitive response-like necrosis when infiltrated into nonhost plants such as tobacco (Nicotiana tabacura L.) (Z.-M. Wei, R.J. Laby, C.H. Zumoff, D.W. Bauer, S.Y. He, A. Collmer, S.V. Beer [1992] Science 257: 85-88). Activity of a 49-kD Mg2+-dependent and Ca2+-independent kinase in tobacco leaves increased 50-fold 15 min after infiltration of harpin from Erwinia amylovora (harpin(Ea)). Much less pronounced and more transient activation was detected in water-infiltrated leaves. Biochemical characteristics of the harpin(Ea)-activated protein kinase (HAPK) activity are consistent with those of the mitogen-activated protein kinase family. HAPK is cytosolic and phosphorylates myelin basic protein on serine/threonine residues. Treatment with a protein tyrosine phosphatase completely eliminated HAPK activity, suggesting that tyrosine phosphorylation is required for posttranslational activation. Sustained HAPK activation after cycloheximide treatment implies that HAPK may be negatively regulated by a translation-dependent mechanism. The extracellular Ca2+ chelator EGTA or the protein kinase inhibitor K252a, infiltrated in planta together with harpin(Ea), partially blocked HAPK activation. The Ca2+-channel blocker La3+ had no effect on HAPK activation, suggesting that phosphorylation events precede and/or do not depend on the entry of extracellular Ca2+ into the cell. These results suggest that early signal transduction events during harpin(Ea)induced hypersensitive response elicitation depend in part on the activation of HAPK.

Original languageEnglish (US)
Pages (from-to)853-861
Number of pages9
JournalPlant physiology
Volume115
Issue number2
DOIs
StatePublished - Jan 1 1997

Fingerprint

Erwinia amylovora
Myelin Basic Protein
protein kinases
Protein Kinases
Tobacco
tobacco
leaves
calcium
hypersensitive response
phosphorylation
Phosphorylation
Protein Tyrosine Phosphatases
Bacterial Proteins
protein-tyrosine-phosphatase
myelin basic protein
Egtazic Acid
bacterial proteins
Threonine
Cycloheximide
Protein Kinase Inhibitors

ASJC Scopus subject areas

  • Physiology
  • Genetics
  • Plant Science

Cite this

Rapid and transient activation of a myelin basic protein kinase in tobacco leaves treated with harpin from Erwinia amylovora. / Ádám, Attila L.; Pike, Sharon; Hoyos, M. Elizabeth; Stone, Julie M.; Walker, John C.; Novacky, Anton.

In: Plant physiology, Vol. 115, No. 2, 01.01.1997, p. 853-861.

Research output: Contribution to journalArticle

Ádám, Attila L. ; Pike, Sharon ; Hoyos, M. Elizabeth ; Stone, Julie M. ; Walker, John C. ; Novacky, Anton. / Rapid and transient activation of a myelin basic protein kinase in tobacco leaves treated with harpin from Erwinia amylovora. In: Plant physiology. 1997 ; Vol. 115, No. 2. pp. 853-861.
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