Intracellular localization and partial amino acid sequence of a stress-inducible 40-kDa protein in HeLa cells.
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.
Hattori
H
H
Department of Oral Surgery, Nagoya University School of Medicine, Japan.
Liu
Y C
YC
Tohnai
I
I
Ueda
M
M
Kaneda
T
T
Kobayashi
T
T
Tanabe
K
K
Ohtsuka
K
K
D000595:Amino Acid Sequence; D000906:Antibodies; D005455:Fluorescent Antibody Technique; D006367:HeLa Cells / Q000737:chemistry* / Q000648:ultrastructure; D006360:Heat-Shock Proteins / Q000737:chemistry* / Q000302:isolation & purification*; D006358:Hot Temperature; D006801:Humans; D008969:Molecular Sequence Data; D012689:Sequence Homology, Nucleic Acid
D000906:Antibodies; D006360:Heat-Shock Proteins