Identification and characterization of rDJL, a novel member of the DnaJ protein family, in rat testis

FEBS Lett. 2005 Oct 24;579(25):5734-40. doi: 10.1016/j.febslet.2005.09.046.


Applying the method of segmentation of seminiferous tubules combined with DDRT-PCR and cDNA library screening, a novel DnaJ homologue, rDJL was identified in rat testis. The reading frame encodes a protein of 223 amino acid residues containing J domain in the NH2 terminal region. rDJL gene is expressed mainly in testis and rDJL protein was immunolocalized notably in the acrosome region of spermatozoa. Immunoprecipitation experiments showed that rDJL interacted with Hsc70 and clathrin protein. When CHO cells were treated with EGF, rDJL and clathrin protein were found to be colocalized and be concentrated as endosome vesicles. The present findings suggest that rDJL functions as co-chaperone to Hsc70, participates in vesicular trafficking and may play an important role in acrosomogenesis.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Acrosome / chemistry
  • Acrosome / metabolism
  • Amino Acid Sequence
  • Animals
  • Base Sequence
  • CHO Cells
  • Clathrin / metabolism
  • Cricetinae
  • Cricetulus
  • Endosomes / chemistry
  • Male
  • Molecular Chaperones / analysis
  • Molecular Chaperones / genetics*
  • Molecular Chaperones / metabolism*
  • Molecular Sequence Data
  • Rats
  • Spermatozoa / chemistry
  • Spermatozoa / metabolism*
  • Testis / cytology
  • Testis / metabolism*
  • Vesicular Transport Proteins / analysis
  • Vesicular Transport Proteins / genetics*
  • Vesicular Transport Proteins / metabolism*


  • Clathrin
  • Molecular Chaperones
  • Samd13 protein, rat
  • Vesicular Transport Proteins