TAILIEUCHUNG - Báo cáo Y học: Mydj2 as a potent partner of hsc70 in mammalian cells

Dj2 is a member of the DnaJ family of proteins, which regulate the chaperoning functionof the isolated a monkey cDNA dj2 clone corresponding to the large mRNA species encoded by the gene. This mRNA differs from the small mRNAproduced 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. | Eur. J. Biochem. 269 1553-1560 2002 FEBS 2002 Mydj2 as a potent partner of hsc70 in mammalian cells Petros Bozidis loannis Lazaridis Gerassimos N. Pagoulatos and Charalampos E. Angelidis Laboratory of General Biology Medical School University of loannina Greece 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. Keywords DnaJ homologue dj2 heat shock cochaperone nanomachine. It is widely accepted today that the eukaryotic DnaJ homologs consist a family of proteins which in combination with the hsp70 family members make up the basic molecular chaperone machinery of the mammalian cell 1 . The members of the above gene families work together in a variety of cellular processes including protein folding during which the hsp70s bind unfolded partially folded or denatured polypeptide substrates and assist their renaturation through a cycle of binding and release regulated by their DnaJ cochaperones 2 3 . Based on the existense of three dinstict domains namely the highly conserved J domain consisting of approximately 70 amino acids and known to mediate the hsp70 binding the glycine phenylalanine G F rich region which possibly acts as a flexible linker and the cysteine rich region C domain which resembles a .

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