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Identification and characterization of rDJL, a novel member of the DnaJ protein family, in rat testis
Author(s) -
Yang Chunbo,
Miao Shiying,
Zong Shudong,
Koide Samuel S.,
Wang Linfang
Publication year - 2005
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2005.09.046
Subject(s) - immunoprecipitation , biology , open reading frame , microbiology and biotechnology , clathrin , complementary dna , endosome , chaperone (clinical) , two hybrid screening , co chaperone , gene , peptide sequence , heat shock protein , biochemistry , endocytosis , hsp70 , receptor , pathology , intracellular , medicine
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.