Hattori H, Liu Y C, Tohnai I, Ueda M, Kaneda T, Kobayashi T, Tanabe K, Ohtsuka K
Department of Oral Surgery, Nagoya University School of Medicine, Japan.
Cell Struct Funct. 1992 Feb;17(1):77-86. doi: 10.1247/csf.17.77.
We earlier discovered a novel 40-kDa protein (hsp40) induced by heat shock and other stresses in mammalian and avian cells. In this report, we purified the hsp40 in HeLa cells, using modified two-dimensional gel electrophoresis, and determined the amino terminal amino acid sequence of this protein. The hsp40 is homologous to DnaJ, an Escherichia coli heat-shock protein, as well as to DnaJ-homologous proteins in yeast such as SCJ1, Sec63/Np11, YDJ1 and SIS1. Indirect immunofluorescence staining using an anti-hsp40 polyclonal antibody demonstrated that hsp40 was localized faintly throughout the cell in non-heat-shocked cells and was accumulated in nuclei and nucleoli in heat-shocked cells. The intracellular localization of hsp40 was very similar to that of hsp70, suggesting that these two hsps colocalize in heat-shocked HeLa cells.
我们之前在哺乳动物和鸟类细胞中发现了一种由热休克和其他应激诱导产生的新型40 kDa蛋白（hsp40）。在本报告中，我们使用改良的二维凝胶电泳法在HeLa细胞中纯化了hsp40，并确定了该蛋白的氨基末端氨基酸序列。hsp40与大肠杆菌热休克蛋白DnaJ以及酵母中的DnaJ同源蛋白如SCJ1、Sec63/Np11、YDJ1和SIS1同源。使用抗hsp40多克隆抗体进行的间接免疫荧光染色表明，在未受热休克的细胞中，hsp40在整个细胞中微弱定位，而在受热休克的细胞中，hsp40积累在细胞核和核仁中。hsp40的细胞内定位与hsp70非常相似，这表明这两种热休克蛋白在受热休克的HeLa细胞中共定位。
