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Human cDNA encoding DnaJ protein homologue

S Oh1, A Iwahori, S Kato

  • 1Sagami Chemical Research Center, Kanagawa, Japan.

Biochimica Et Biophysica Acta
|July 18, 1993
PubMed
Summary
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Researchers identified a human DnaJ homologue, a protein crucial for cellular processes, by cloning its complementary DNA (cDNA) from fibrosarcoma cells. This finding advances understanding of heat shock proteins in human biology.

Area of Science:

  • Molecular Biology
  • Genetics
  • Human Protein Research

Background:

  • DnaJ proteins are essential molecular chaperones involved in protein folding and cellular stress response.
  • Homologues of DnaJ are found across various species, indicating conserved functions.

Purpose of the Study:

  • To identify and characterize the human homologue of the DnaJ protein.
  • To isolate the complementary DNA (cDNA) encoding this human DnaJ-like protein.

Main Methods:

  • Cloning of cDNA from a human fibrosarcoma HT-1080 cell line library.
  • Sequence analysis to determine protein identity and conserved domains.
  • Comparison of the human sequence with known DnaJ proteins from Escherichia coli and yeast.

Main Results:

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  • Successfully cloned a cDNA encoding a 397-amino acid protein.
  • The human protein sequence exhibited significant identity (38.2% with E. coli, 47.2% with yeast) to known DnaJ proteins.
  • The cloned sequence contained conserved N-terminal domains and characteristic Cys-X-X-Cys-X-Gly-X-Gly motifs of the DnaJ family.

Conclusions:

  • The cloned cDNA represents the human homologue of DnaJ.
  • This discovery provides a crucial tool for studying DnaJ protein functions in human cells.
  • Further research can explore the role of human DnaJ in cellular processes and disease.