Open AccessMydj2 as a potent partner of hsc70 in mammalian cells
Author(s) -
Bozidis Petros,
Lazaridis Ioannis,
Pagoulatos Gerassimos N,
Angelidis Charalampos E.
Publication year - 2002
Publication title -
european journal of biochemistry
Language(s) - English
Resource type - Journals
eISSN - 1432-1033
pISSN - 0014-2956
DOI - 10.1046/j.1432-1033.2002.02807.x
Subject(s) - messenger rna , untranslated region , biology , complementary dna , gene , clone (java method) , function (biology) , heat shock protein , hsp70 , hspa12a , microbiology and biotechnology , gene expression , genetics
Dj2 is a member of the DnaJ family of proteins, which regulate the chaperoning function of the hsp70s. We isolated a monkey cDNA dj2 clone corresponding to the large mRNA species encoded by the gene. This mRNA differs from the small mRNA produced by the same gene in that it contains a long 3′ untranslated region. Both messages were found to be equally stable and to produce the same protein, which is susceptible to farnesylation. Studies in mouse tissues and various cell lines revealed that these messages and their products are differentially expressed. Surprisingly, we found that only the nonfarnesylated form of dj2 is capable of translocating to the cell nucleus, especially after heat shock. Finally, based on protein interaction studies, our results indicate that dj2 is a specific partner for hsc70 and not for␣hsp70.