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Plant Physiol, March 2001, Vol. 125, pp. 1429-1441
The Salt Stress-Inducible Protein Kinase
Gene, Esi47, from the Salt-Tolerant Wheatgrass
Lophopyrum elongatum Is Involved in Plant Hormone
Signaling1
Wei
Shen,
Aurelio
Gómez-Cadenas,2
Elizabeth L.
Routly,
Tuan-Hua David
Ho,
John A.
Simmonds, and
Patrick J.
Gulick*
Centre for Structural and Functional Genomics and Department of
Biology, Concordia University, 1455 de Maisonneuve Boulevard
West, Montreal, Quebec, Canada H3G 1M8 (W.S., E.L.R., P.J.G.);
Department of Biology, Washington University, St. Louis, Missouri 63130 (A.G.-C., T.-H.D.H.); and Agriculture and AgriFood Canada, Eastern
Cereal and Oilseed Research Centre, Central Experimental Farm, Ottawa,
Ontario, Canada K1A 0C6 (E.L.R., J.A.S.)
Protein kinases play a central role in signal transduction in all
organisms and to study signal transduction in response to salt stress
we have identified and characterized a gene encoding a protein kinase
that is induced by salt stress and abscisic acid (ABA) in the
salt-tolerant wild wheatgrass Lophopyrum elongatum (Host) A. Love. The product of the early salt stress-induced gene, Esi47, was found to belong to the "novel Arabidopsis
protein kinase" group of plant serine/threonine protein kinases.
Transient gene expression assays in barley aleurone tissue showed
Esi47 to suppress the gibberellin induction of the
barley low-pI  -amylase gene promoter, thus providing evidence for
the role of this protein kinase gene in plant hormone signaling.
Esi47 contains a small upstream open reading frame in
the 5'-untranslated region of its transcript that is implicated in
mediating the repression of the basal level of the gene expression and
in regulating the ABA inducibility of the gene, as shown in the
transient gene expression assay in maize callus. Three Arabidopsis
homologs of Esi47 were identified, and different members
of this clade of genes showed differential patterns of regulation by
salt stress and ABA in Arabidopsis roots and leaves. At least one of
the Arabidopsis homologs contains a small open reading frame in its
5'-untranslated region, indicating that the unusual regulatory
mechanism identified in Esi47 may be widely conserved.
1
This work was supported by the Natural Sciences
and Engineering Council of Canada and the Fonds pour la Formation des
Chercheurs et l'Aide à la Recherche (grants to P.J.G.). W.S. was
supported by a postgraduate scholarship from the Natural Sciences and
Engineering Council of Canada.
2
Present address: Department of Experimental Sciences,
Universitat Jaume I, 12071 Catellon, Spain.
*
Corresponding author; e-mail pgulick{at}alcor.concordia.ca; fax
514-848-2881.
© 2001 American Society of Plant Physiologists
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