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THE PLANT CELL, Vol 5, Issue 1 87-96, Copyright © 1993 by American Society of Plant Biologists
MsERK1: A Mitogen-Activated Protein Kinase from a Flowering Plant
B. Duerr, M. Gawienowski, T. Ropp and T. Jacobs
Department of Plant Biology, University of Illinois, Urbana, Illinois 61801
The induction of proliferation and differentiation in cultured mammalian
cells is mediated by a cascade of protein phosphorylations. A key enzyme in
this signaling pathway is mitogen-activated protein (MAP) kinase (or ERK,
extracellular signal-regulated kinase). We report the recovery of a
full-length cDNA clone encoding a MAP kinase from alfalfa. We have named
the 44-kD protein encoded by this clone MsERK1. Recombinant MsERK1
(rMsERK1), when overexpressed in Escherichia coli, is recognized by
antibodies raised against MAP kinases from rat, Xenopus, and sea star and
by anti-phosphotyrosine antibodies. Site-directed mutagenesis of MsERK1
demonstrated that Tyr-215 is either directly or indirectly responsible for
recognition of the protein by anti-phosphotyrosine antibodies. Semipurified
rMsERK1 phosphorylated itself and a model substrate, myelin basic protein,
in vitro, but the Tyr-215 mutant did neither. Genomic DNA gel blot analysis
suggested that the gene that encodes MsERK1 is either a member of a small
multigene family or a member of a polymorphic allelic series in alfalfa.
Because MAP kinase activation has been associated with mitotic stimulation
in animal systems, such an enzyme may play a role in the mitogenic
induction of symbiotic root nodules on alfalfa by Rhizobium signal
molecules.
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