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The detailed mechanism of eukaryotic 20S proteasome assembly is currently unknown. In the present study, we demonstrate that the 20S proteasome subunits α4 and α7 interact with each other as well as all the α-subunits in vivo and in vitro. The N-terminal parts of α4 and α7 are essential for these newly discovered interactions in vitro. Glycerol gradient centrifugation of soluble extracts of HEK293...
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