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TitleHigh resolution structures define divergent and convergent mechanisms of archaeal proteasome activation.
Journal, issue, pagesCommun Biol, Vol. 6, Issue 1, Page 733, Year 2023
Publish dateJul 15, 2023
AuthorsJanelle J Y Chuah / Matthew S Rexroad / David M Smith /
PubMed AbstractConsidering the link between neurodegenerative diseases and impaired proteasome function, and the neuro-protective impact of enhanced proteasome activity in animal models, it's crucial to understand ...Considering the link between neurodegenerative diseases and impaired proteasome function, and the neuro-protective impact of enhanced proteasome activity in animal models, it's crucial to understand proteasome activation mechanisms. A hydrophobic-tyrosine-any residue (HbYX) motif on the C-termini of proteasome-activating complexes independently triggers gate-opening of the 20S core particle for protein degradation; however, the causal allosteric mechanism remains unclear. Our study employs a structurally irreducible dipeptide HbYX mimetic to investigate the allosteric mechanism of gate-opening in the archaeal proteasome. High-resolution cryo-EM structures pinpoint vital residues and conformational changes in the proteasome α-subunit implicated in HbYX-dependent activation. Using point mutations, we simulated the HbYX-bound state, providing support for our mechanistic model. We discerned four main mechanistic elements triggering gate-opening: 1) back-loop rearrangement adjacent to K66, 2) intra- and inter- α subunit conformational changes, 3) occupancy of the hydrophobic pocket, and 4) a highly conserved isoleucine-threonine pair in the 20S channel stabilizing the open and closed states, termed the "IT switch." Comparison of different complexes unveiled convergent and divergent mechanism of 20S gate-opening among HbYX-dependent and independent activators. This study delivers a detailed molecular model for HbYX-dependent 20S gate-opening, enabling the development of small molecule proteasome activators that hold promise to treat neurodegenerative diseases.
External linksCommun Biol / PubMed:37454196 / PubMed Central
MethodsEM (single particle)
Resolution1.94 - 2.28 Å
Structure data

28876

8f66

EMDB-28876, PDB-8f66:
Thermoplasma acidophilum 20S proteasome - L81Y mutation in alpha subunit
Method: EM (single particle) / Resolution: 2.28 Å

28878

8f6a

EMDB-28878, PDB-8f6a:
Thermoplasma acidophilum 20S proteasome - wild type
Method: EM (single particle) / Resolution: 2.06 Å

28906

8f7k

EMDB-28906, PDB-8f7k:
Thermoplasma acidophilum 20S proteasome - wild type bound to ZYA
Method: EM (single particle) / Resolution: 1.94 Å

Chemicals

ChemComp-XIB:
N-[(benzyloxy)carbonyl]-L-tyrosyl-D-alanine

Source
  • thermoplasma acidophilum (acidophilic)
KeywordsHYDROLASE / Protease / threonine protease / endopeptidase activity

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