I. Iliopoulos et al., THE DNAJ60 GENE OF DROSOPHILA-MELANOGASTER ENCODES A NEW MEMBER OF THE DNAJ FAMILY OF PROTEINS, Biological chemistry, 378(10), 1997, pp. 1177-1181
In eukaryotes the DnaJ homolog constitute a family of proteins with di
verse functions which all appear to involve the chaperone activity of
Hsp70. Here, we report the molecular characterization of DnaJ60, a gen
e located at 60C on the right arm of the second chromosome of Drosophi
la melanogaster and encoding a putative protein of 217 amino acids wit
h a molecular mass of 27.7-kDa and a pI of 10.5. The N-terminal region
of the DnaJ60 protein displays a significant sequence similarity with
the J domain of DnaJ proteins and contains a centrally located hydrop
hobic segment suggesting the occurrence of a membrane spanning domain.
Northern blot analysis detected a 0.75-kb transcript which is weakly
expressed in embryos, larvae and females but intensively expressed in
adult males. In situ localization revealed that the DnaJ60 transcript
is highly expressed in male testes and the ejaculary bulb but at an un
detectable level in ovaries suggesting that the DnaJ60 protein may pla
y an important function during spermatogenesis and/or in the male geni
tal tract.