Zhang S, Klessig D F
Waksman Institute and Department of Molecular Biology and Biochemistry, Rutgers, State University of New Jersey, Piscataway, NJ 08854-8020, USA.
Proc Natl Acad Sci U S A. 1998 Jun 9;95(12):7225-30. doi: 10.1073/pnas.95.12.7225.
It has been demonstrated that both salicylic acid and fungal elicitors activate a 48-kDa mitogen-activated protein kinase termed salicylic acid-induced protein kinase (SIPK) in tobacco suspension cells. Here, we show that infiltration of these agents into tobacco leaves also activates SIPK. Of particular interest, infiltration of water alone activated a kinase of the same size, possibly because of wounding and/or osmotic stresses. The kinetics of kinase activation, however, differ for these different treatments. Various mechanical stresses, including cutting and wounding by abrasion, also activated a 48-kDa kinase. By using an immune-complex kinase assay with antibodies specific for SIPK or wounding-induced protein kinase, we demonstrate that this wounding-activated 48-kDa kinase is SIPK, rather than wounding-induced protein kinase, as reported [Seo, S., Okamoto, M., Seto, H., Ishizuka, K., Sano, H. & Ohashi, Y. (1995) Science 270, 1988-1992]. Activation of SIPK after wounding was associated with tyrosine phosphorylation but not with increases in SIPK mRNA or protein levels. Thus, the same mitogen-activated protein kinase, SIPK, appears to facilitate signaling for two distinct pathways that lead to disease resistance responses and wounding responses.
业已证明,水杨酸和真菌激发子均可在烟草悬浮细胞中激活一种48 kDa的丝裂原活化蛋白激酶,即水杨酸诱导蛋白激酶(SIPK)。在此,我们表明,将这些试剂渗入烟草叶片也能激活SIPK。特别有趣的是,仅用水渗入就能激活相同大小的一种激酶,这可能是由于创伤和/或渗透胁迫所致。然而,这些不同处理的激酶激活动力学有所不同。包括切割和磨损创伤在内的各种机械胁迫也能激活一种48 kDa的激酶。通过使用针对SIPK或创伤诱导蛋白激酶的特异性抗体进行免疫复合物激酶分析,我们证明这种创伤激活的48 kDa激酶是SIPK,而不是如报道的创伤诱导蛋白激酶[Seo, S., Okamoto, M., Seto, H., Ishizuka, K., Sano, H. & Ohashi, Y. (1995) Science 270, 1988 - 1992]。创伤后SIPK的激活与酪氨酸磷酸化有关,但与SIPK mRNA或蛋白水平的增加无关。因此,同一种丝裂原活化蛋白激酶SIPK似乎促进了导致抗病反应和创伤反应的两条不同途径的信号传导。