ZmMPK6, a novel maize MAP kinase that interacts with 14-3-3 proteins.
Although an increasing body of evidence indicates that plant MAP kinases are involved in a number of cellular processes, such as cell cycle regulation and cellular response to abiotic stresses, hormones and pathogen attack, very little is known about their biochemical properties and regulation mechanism. In this paper we report on the identification and characterization of a novel member of the MAP kinase family from maize, ZmMPK6. The amino acid sequence reveals a high degree of identity with group D plant MAP kinases. Recombinant ZmMPK6, expressed in Escherichia coli, is an active enzyme able to autophosphorylate. Remarkably, ZmMPK6 interacts in vitro with GF14-6, a maize 14-3-3 protein and the interaction is dependent on autophosphorylation. The interacting domain of ZmMPK6 is on the C-terminus and is comprised between amino acid 337 and amino acid 467. Our results represent the first evidence of an interaction between a plant MAP kinase and a 14-3-3 protein. Possible functional roles of this association in vivo are discussed.
Lalle
Marco
M
Department of Biology, University of Rome "Tor Vergata", via della Ricerca Scientifica, 100133 Rome, Italy.
Visconti
Sabina
S
Marra
Mauro
M
Camoni
Lorenzo
L
Velasco
Riccardo
R
Aducci
Patrizia
P
D048948:14-3-3 Proteins / Q000235:genetics / Q000378:metabolism*; D000595:Amino Acid Sequence; D020224:Expressed Sequence Tags; D015971:Gene Expression Regulation, Enzymologic; D018506:Gene Expression Regulation, Plant; D020928:Mitogen-Activated Protein Kinases / Q000235:genetics / Q000378:metabolism*; D008969:Molecular Sequence Data; D011485:Protein Binding; D016415:Sequence Alignment; D017386:Sequence Homology, Amino Acid; D003313:Zea mays / Q000201:enzymology* / Q000235:genetics
D048948:14-3-3 Proteins; D020928:Mitogen-Activated Protein Kinases