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TitleStructure of Blm10:13S proteasome intermediate reveals parallel assembly pathways for the proteasome core particle.
Journal, issue, pagesbioRxiv, Year 2024
Publish dateNov 5, 2024
AuthorsMandeep Kaur / Xiang Chen / Stella Y Lee / Tyler M Weaver / Bret D Freudenthal / Kylie J Walters / Jeroen Roelofs /
PubMed AbstractProteasomes are formed by chaperone-assisted assembly of core particles (CPs) and regulatory particles (RPs). The CP chaperone dimer Pba1/Pba2 binds early to proteasome subunits, and is thought to be ...Proteasomes are formed by chaperone-assisted assembly of core particles (CPs) and regulatory particles (RPs). The CP chaperone dimer Pba1/Pba2 binds early to proteasome subunits, and is thought to be replaced by Blm10 to form Blm10:CP, which promotes ATP-independent degradation of disordered proteins. Here, we present evidence of distinct parallel assembly pathways for CP by solving five cryo-EM structures including a Blm10:13S pre-assembly intermediate. Our data conflict with the current model of Blm10 and Pba1/Pba2 sequential activity in a single assembly pathway, as we find their CP binding is mutually exclusive and both are present on early and late assembly intermediates. CP affinity for Pba1/Pba2 is reduced during maturation, promoting Pba1/Pba2 release. We find Blm10 undergoes no such affinity switch, suggesting this pathway predominantly yields mature Blm10-bound CP. Altogether, our findings conflict with the current paradigm of sequential CP binding to instead indicate parallel assembly pathways by Pba1/Pba2 and Blm10.
External linksbioRxiv / PubMed:39574619 / PubMed Central
MethodsEM (single particle)
Resolution2.84 Å
Structure data

46461

9d0t

EMDB-46461, PDB-9d0t:
Proteasome core particle assembly intermediate Blm10:13S purified from Saccharomyces cerevisiae
Method: EM (single particle) / Resolution: 2.84 Å

Source
  • saccharomyces cerevisiae (brewer's yeast)
KeywordsHYDROLASE / Proteasome / assembly chaperone / Blm10 / PA200 / Blm10-13S / Pba1 / CP

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