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, M., Visconti, S., Marra, M., Camoni, L., Velasco, R., Aducci, P. (2005). ZmMPK6, a novel maize MAP kinase that interacts with 14-3-3 proteins. PLANT MOLECULAR BIOLOGY, 59(5), 713-722 [10.1007/s11103-005-0862-x].

ZmMPK6, a novel maize MAP kinase that interacts with 14-3-3 proteins

VISCONTI, SABINA;MARRA, MAURO;CAMONI, LORENZO;ADUCCI, PATRIZIA
2005-01-01

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.
2005
Pubblicato
Rilevanza internazionale
Articolo
Sì, ma tipo non specificato
Settore BIO/04 - FISIOLOGIA VEGETALE
English
Con Impact Factor ISI
14-3-3 protein; MAP kinase; Protein-protein interaction; Zea mays
Lalle, M., Visconti, S., Marra, M., Camoni, L., Velasco, R., Aducci, P. (2005). ZmMPK6, a novel maize MAP kinase that interacts with 14-3-3 proteins. PLANT MOLECULAR BIOLOGY, 59(5), 713-722 [10.1007/s11103-005-0862-x].
Lalle, M; Visconti, S; Marra, M; Camoni, L; Velasco, R; Aducci, P
Articolo su rivista
File in questo prodotto:
Non ci sono file associati a questo prodotto.

I documenti in IRIS sono protetti da copyright e tutti i diritti sono riservati, salvo diversa indicazione.

Utilizza questo identificativo per citare o creare un link a questo documento: https://hdl.handle.net/2108/34928
Citazioni
  • ???jsp.display-item.citation.pmc??? 11
  • Scopus ND
  • ???jsp.display-item.citation.isi??? 31
social impact