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TitleThe YΦ motif defines the structure-activity relationships of human 20S proteasome activators.
Journal, issue, pagesNat Commun, Vol. 13, Issue 1, Page 1226, Year 2022
Publish dateMar 9, 2022
AuthorsKwadwo A Opoku-Nsiah / Andres H de la Pena / Sarah K Williams / Nikita Chopra / Andrej Sali / Gabriel C Lander / Jason E Gestwicki /
PubMed AbstractThe 20S proteasome (20S) facilitates turnover of most eukaryotic proteins. Substrate entry into the 20S first requires opening of gating loops through binding of HbYX motifs that are present at the C- ...The 20S proteasome (20S) facilitates turnover of most eukaryotic proteins. Substrate entry into the 20S first requires opening of gating loops through binding of HbYX motifs that are present at the C-termini of certain proteasome activators (PAs). The HbYX motif has been predominantly characterized in the archaeal 20S, whereas little is known about the sequence preferences of the human 20S (h20S). Here, we synthesize and screen ~120 HbYX-like peptides, revealing unexpected differences from the archaeal system and defining the h20S recognition sequence as the Y-F/Y (YФ) motif. To gain further insight, we create a functional chimera of the optimized sequence, NLSYYT, fused to the model activator, PA26. A cryo-EM structure of PA26-h20S is used to identify key interactions, including non-canonical contacts and gate-opening mechanisms. Finally, we demonstrate that the YФ sequence preferences are tuned by valency, allowing multivalent PAs to sample greater sequence space. These results expand the model for termini-mediated gating and provide a template for the design of h20S activators.
External linksNat Commun / PubMed:35264557 / PubMed Central
MethodsEM (single particle)
Resolution3.0 Å
Structure data

22259

6xmj

EMDB-22259, PDB-6xmj:
Human 20S proteasome bound to an engineered 11S (PA26) activator
Method: EM (single particle) / Resolution: 3.0 Å

Source
  • homo sapiens (human)
  • trypanosoma brucei (eukaryote)
KeywordsHYDROLASE / 11S-bound / 20S proteasome

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