Identity of an ABA-activated 46 kDa mitogen-activated protein kinase from Zea mays leaves: Partial purification, identification and characterization

Haidong Ding, Aying Zhang, Jinxiang Wang, Rui Lu, Hong Zhang, Jianhua ZHANG, Mingyi Jiang*

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

33 Citations (Scopus)

Abstract

Mitogen-activated protein kinase (MAPK) cascades have been shown to be important components in abscisic acid (ABA) signal transduction pathway. In this study, a 46 kDa MAPK (p46MAPK) induced by ABA was partially purified from maize (Zea mays) by Q-Sepharose FF, Phenyl-Sepharose FF, Resource Q, Mono QTM 5/50 GL, poly-l-lysine-agarose, and Superdex 75 prep-grade columns, and was identified as ZmMAPK5 (gi|4239889) by the matrix-assisted laser desorption/ionization time-of-flight/time-of-flight (MALDI-TOF/TOF) mass spectrometry. Furthermore, the kinase showed optimal activity at pH 8.0, 30°C, and 10 mM MgCl2; the K m for myelin basic protein (MBP) substrate and ATP were 0.13 μg μl-1 and 62 μM, respectively. MBP was the preferred substrate, of which the threonine residue was phosphorylated. Finally, the kinase was found to respond to diverse extracelluar stimuli. These results enable us to further reveal the function of the ZmMAPK5 in ABA signaling.

Original languageEnglish
Pages (from-to)239-251
Number of pages13
JournalPlanta
Volume230
Issue number2
DOIs
Publication statusPublished - Jul 2009

Scopus Subject Areas

  • Genetics
  • Plant Science

User-Defined Keywords

  • Abscisic acid
  • Mass spectrometry
  • Mitogen-activated protein kinase
  • Protein purification
  • Zea

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