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Intracellular localization and partial amino acid sequence of a stress-inducible 40-kDa protein in HeLa cells.

Hattori H., Liu Y.-C., Tohnai I., Ueda M., Kaneda T., Kobayashi T., Tanabe K., Ohtsuka K.

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.

Cell Struct. Funct. 17:77-86(1992) [PubMed] [Europe PMC]

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