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TitleBlm10 and PI31 comprise a failsafe mechanism for proteasome inhibition.
Journal, issue, pagesProc Natl Acad Sci U S A, Vol. 123, Issue 30, Page e2611708123, Year 2026
Publish dateJul 28, 2026
AuthorsDarlene Fung / Shaun Rawson / Richard M Walsh / Erignacio Fermin Perez / Urte Venclovaite / Tamayanthi Rajakumar / Benjamin Velez / John Hanna /
PubMed AbstractBlm10 (PA200 in mammals) is an evolutionarily conserved regulator of the proteasome's core particle (CP), a barrel-shaped complex that houses six individual protease subunits. Despite decades of ...Blm10 (PA200 in mammals) is an evolutionarily conserved regulator of the proteasome's core particle (CP), a barrel-shaped complex that houses six individual protease subunits. Despite decades of study, Blm10's function has remained unresolved. Here, we provide structural, biochemical, and genetic evidence that yeast Blm10 inhibits the proteasome and that it does so in cooperation with a second proteasome inhibitor, PI31 (also known as Fub1). Both proteins are highly enriched in CPs with abnormal subunit composition, suggesting that Blm10 and PI31 may function to neutralize aberrant proteasomes. We report an unexpected proteasome configuration in which Blm10's dome-like structure completely encases PI31's N-terminal domain, which sits outside and atop the CP, while PI31's C-terminal domain is present inside the CP, simultaneously inhibiting all six active sites. These Blm10/PI31-bound CP are strongly deficient in degradation of both proteins and small peptides, and loss of both proteins results in strongly synergistic genetic phenotypes in vivo. These data suggest that Blm10 and PI31 constitute a partially redundant failsafe system for proteasome inhibition.
External linksProc Natl Acad Sci U S A / PubMed:42485378 / PubMed Central
MethodsEM (single particle)
Resolution3.2 - 4.1 Å
Structure data

75163

10gx

EMDB-75163, PDB-10gx:
Yeast Blm10 apo Structure
Method: EM (single particle) / Resolution: 3.2 Å

75294

10mt

EMDB-75294, PDB-10mt:
C2 symmetry expanded and subtracted 20S Proteasome, Blm10, Fub1 Complex Halfmer
Method: EM (single particle) / Resolution: 3.7 Å

75334

10og

EMDB-75334, PDB-10og:
20S Alpha 3 Deletion proteasome core particle in complex with Fub1 and Blm10
Method: EM (single particle) / Resolution: 4.1 Å

75393

10qt

EMDB-75393, PDB-10qt:
C2 expanded and subtracted 20S Alpha 3 Deletion proteasome core particle in complex with Blm10, Halfmer
Method: EM (single particle) / Resolution: 3.4 Å

75436

10sj

EMDB-75436, PDB-10sj:
20S Alpha 3 Deletion proteasome core particle in complex with Blm10
Method: EM (single particle) / Resolution: 3.7 Å

Source
  • saccharomyces cerevisiae (brewer's yeast)
  • saccharomyces cerevisiae s288c (yeast)
KeywordsPROTEIN BINDING / Proteasome Regulator / HYDROLASE / 20S Proteasome / Proteasome Inhibitor

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