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Chaperonin TRiC/CCT Recognizes Fusion Oncoprotein AML1-ETO through Subunit-Specific Interactions

Cited 8 time in Web of Science Cited 10 time in Scopus
Authors

Roh, Soung-Hun; Kasembeli, Moses M.; Galaz-Montoya, Jesus G.; Chiu, Wah; Tweardy, David J.

Issue Date
2016-06
Publisher
Biophysical Society
Citation
Biophysical Journal, Vol.110 No.11, pp.2377-2385
Abstract
AML1-ETO is the translational product of a chimeric gene created by the stable chromosome translocation t (8;21)(q22;q22). It causes acute myeloid leukemia (AML) by dysregulating the expression of genes critical for myeloid cell development and differentiation and recently has been reported to bind multiple subunits of the mammalian cytosolic chaperonin TRiC (or CCT), primarily through its DNA binding domain (AML1-175). Through these interactions, TRiC plays an important role in the synthesis, folding, and activity of AML1-ETO. Using single-particle cryo-electron microscopy, we demonstrate here that a folding intermediate of AML1-ETO's DNA-binding domain (AML1-175) forms a stable complex with apo-TRiC. Our structure reveals that AML1-175 associates directly with a specific subset of TRiC subunits in the open conformation.
ISSN
0006-3495
URI
https://hdl.handle.net/10371/203190
DOI
https://doi.org/10.1016/j.bpj.2016.04.045
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  • College of Natural Sciences
  • School of Biological Sciences
Research Area Cryogenic Electron Microscopy (Cryo-EM), Structural Biology, 분자생물학, 생물물리학, 생화학

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