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- W3048665325 endingPage "1217.e4" @default.
- W3048665325 startingPage "1206" @default.
- W3048665325 abstract "The 26S proteasome is specialized for regulated protein degradation and formed by a dynamic regulatory particle (RP) that caps a hollow cylindrical core particle (CP) where substrates are proteolyzed. Its diverse substrates unify as proteasome targets by ubiquitination. We used cryogenic electron microscopy (cryo-EM) to study how human 26S proteasome interacts with M1-linked hexaubiquitin (M1-Ub6) unanchored to a substrate and E3 ubiquitin ligase E6AP/UBE3A. Proteasome structures are available with model substrates extending through the RP ATPase ring and substrate-conjugated K63-linked ubiquitin chains present at inhibited deubiquitinating enzyme hRpn11 and the nearby ATPase hRpt4/hRpt5 coiled coil. In this study, we find M1-Ub6 at the hRpn11 site despite the absence of conjugated substrate, indicating that ubiquitin binding at this location does not require substrate interaction with the RP. Moreover, unanchored M1-Ub6 binds to this hRpn11 site of the proteasome with the CP gating residues in both the closed and opened conformational states." @default.
- W3048665325 created "2020-08-18" @default.
- W3048665325 creator A5001710213 @default.
- W3048665325 creator A5021583015 @default.
- W3048665325 creator A5038121623 @default.
- W3048665325 creator A5043093660 @default.
- W3048665325 creator A5054888023 @default.
- W3048665325 creator A5056181739 @default.
- W3048665325 creator A5059250774 @default.
- W3048665325 creator A5063310304 @default.
- W3048665325 creator A5075228460 @default.
- W3048665325 creator A5076768386 @default.
- W3048665325 date "2020-11-01" @default.
- W3048665325 modified "2023-09-27" @default.
- W3048665325 title "Cryo-EM Reveals Unanchored M1-Ubiquitin Chain Binding at hRpn11 of the 26S Proteasome" @default.
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