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    Cell Struct Funct. 1992 Feb;17(1):77-86.

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

    Hattori H, Liu YC, Tohnai I, Ueda M, Kaneda T, Kobayashi T, Tanabe K, Ohtsuka K.

    Department of Oral Surgery, Nagoya University School of Medicine, Japan.

    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.

    PMID: 1586970 [PubMed - indexed for MEDLINE]

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