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In our previous proteomic study, the recombinant yeast YGH2 expressing active human H-ferritin induced cellular iron deficiency and significantly decreased expression of the mitochondria heat shock protein 60(HSP60) whereas other HSPs increased. HSPs are chaperon proteins that promote the folding of proteins and are overexpressed under stress. In the study, we verified the relationship between iron depletion and HSP60 via Northern blot using the iron chelator BIP or
iron supplements. The expression level of the high affinity iron transporter gene FET3 was also examined. Several recombinant strains were compared. The HSP60 expression reduced in the cells of YGH2 cultured for 12 hr. Upon treatment of the control cells with BIP, the expression of HSP60 reduced and FET3 increased. For YGH2 added with Fe2+ or Fe3+ at 0-300μM, changes in the amounts of HSP60 were little while FET3 decreased gradually. Possible explanations for such
discrepancy are that (i) H-ferritins are still functional at the iron concentrations we examined. (ii) H-ferritin may function in a distinctive way in the HSP60 expression. Future study of YGH2 with higher iron levels will assist us to understand the questions.