| Affiliation: | (1) Department of Biology, University of Rome “Tor Vergata”, via della Ricerca Scientifica, 100133 Rome, Italy;(2) Department of Infectious, Parasitic and Immuno-mediated Diseases, Istituto Superiore di Sanita’, Viale Regina Elena 299, 00161 Rome, Italy;(3) Department of Biological and Environmental Studies, University of Sannio, via Port’Arsa 11, 82100 Benevento, Italy;(4) Max Planck Institut fuer Zuechtungsforschung, Carl-von-Linne-Weg 10, 50829 Koeln, Germany;(5) Present address: Istituto Agrario San Michele all’Adige, via Mach 1, 38010 San Michele a/Adige, (TN), Italy |
| Abstract: | 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. |
