Parida Asish Kumar, Mittra Bhabatosh, Das Anath Bandhu, Das Taposh Kumar, Mohanty Prasanna
National Institute for Plant Biodiversity Conservation and Research, Nayapalli, 751015 Bhubaneswar, Orissa, India.
Planta. 2005 Apr;221(1):135-40. doi: 10.1007/s00425-004-1415-2. Epub 2004 Dec 3.
A significant decrease in the amount of a protein, whose migration in two-dimensional gel electrophoresis corresponds to an apparent molecular mass of 23 kDa and pI = 6.5, was observed in leaves of NaCl-treated Bruguiera parviflora (Roxb.) Wt. & Arn. ex Griff. seedlings. This particular salt-sensitive protein, designated as SSP-23, almost disappeared after 45 days of treatment in 400 mM NaCl as compared to untreated seedlings (0 mM NaCl) where the presence of the protein was significant. A polyclonal antibody raised against the 23-kDa protein was used to determine the subcellular localization of this protein in leaves by cross-reaction with proteins from isolated chloroplasts, mitochondria, peroxisomes and cytosol fractions on Western blots. SSP-23 was confirmed to be localized in the cytosol by immunoblotting. The disappearance of SSP-23 as a result of high NaCl treatment suggests that this protein is salt-sensitive and has a possible role in salt adaptation.
在经NaCl处理的小花木榄(Bruguiera parviflora (Roxb.) Wt. & Arn. ex Griff.)幼苗的叶片中,观察到一种蛋白质的量显著减少,该蛋白质在二维凝胶电泳中的迁移对应于表观分子量为23 kDa且pI = 6.5。这种特殊的盐敏感蛋白,命名为SSP - 23,与未处理的幼苗(0 mM NaCl)相比,在400 mM NaCl中处理45天后几乎消失,而在未处理的幼苗中该蛋白的存在是显著的。用针对23 kDa蛋白产生的多克隆抗体通过与来自分离的叶绿体、线粒体、过氧化物酶体和细胞质组分的蛋白质在Western印迹上的交叉反应来确定该蛋白在叶片中的亚细胞定位。通过免疫印迹证实SSP - 23定位于细胞质中。高NaCl处理导致SSP - 23消失,这表明该蛋白对盐敏感,并且在盐适应中可能发挥作用。