TY - JOUR
T1 - Identity of an ABA-activated 46 kDa mitogen-activated protein kinase from Zea mays leaves
T2 - Partial purification, identification and characterization
AU - Ding, Haidong
AU - Zhang, Aying
AU - Wang, Jinxiang
AU - Lu, Rui
AU - Zhang, Hong
AU - ZHANG, Jianhua
AU - Jiang, Mingyi
N1 - Funding Information:
Acknowledgments This work was supported by the National Natural Science Foundation of China (grant nos. 30571122 and 30671247 to M. J.), the Universities Qing-Lan Project of Jiangsu Province (to M. J.), the Graduate Research and Innovation Plan of Jiangsu Province (grant no. CX07B_052Z to H. D.), and the Open Project of the National Key Laboratory of Crop Genetics and Germplasm Enhancement of Nanjing Agricultural University (grant no. ZW2007002 to M. J.).
PY - 2009/7
Y1 - 2009/7
N2 - 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.
AB - 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.
KW - Abscisic acid
KW - Mass spectrometry
KW - Mitogen-activated protein kinase
KW - Protein purification
KW - Zea
UR - http://www.scopus.com/inward/record.url?scp=67649464361&partnerID=8YFLogxK
U2 - 10.1007/s00425-009-0938-y
DO - 10.1007/s00425-009-0938-y
M3 - Journal article
C2 - 19424717
AN - SCOPUS:67649464361
SN - 0032-0935
VL - 230
SP - 239
EP - 251
JO - Planta
JF - Planta
IS - 2
ER -