While known for decades to be the translational product of a chimeric gene created by the stable chromosome translocation t(8;21)(q22;q22), it is not known how AML1-ETO achieves its native and functional conformation or whether this process can be targeted for therapeutic benefit.     ///    "AML1-ETO functions as a rogue transcription factor, altering the expression of genes critical for myeloid cell development and differentiation. "    ///    "Our results suggest that TRiC contributes to AML1-ETO proteostasis through specific interactions between the oncoprotein's DNA-binding domain, which may be targeted for therapeutic benefit. "    ///    "Here, we show that the biosynthesis and folding of the AML1-ETO protein is facilitated by interaction with the essential eukaryotic chaperonin TRiC (or CCT). "    ///    "We demonstrate that a folding intermediate of AML1-ETO binds to TRiC directly, mainly through its ?-strand rich, DNA-binding domain (AML-(1-175)), with the assistance of HSP70. "    ///    Chaperonin TRiC/CCT Modulates the Folding and Activity of Leukemogenic Fusion Oncoprotein AML1-ETO..     ///    " AML1-ETO is the most common fusion oncoprotein causing acute myeloid leukemia (AML), a disease with a 5-year survival rate of only 24%. "