Matias, Ana CatarinaTiago, Maria MargaridaZimmermann, JessicaDohmen, R. JürgenRamos, Paula C.2025-07-222025-07-222025-05-082218-273Xhttp://hdl.handle.net/10400.1/27473A complex composed of Pba3-Pba4 and subunits α5, α6, and α7 is identified as an early intermediate in proteasome core particle assembly in wild-type Saccharomyces cerevisiae cells. The same complex can be reconstituted from recombinantly produced components in vitro. Assembly of α6 and α7 with Pba3-Pba4 depends on the presence of the α5 subunit, the binding of which apparently initiates the formation of this intermediate. Our data suggest the following order of events: first, Pba3-Pba4 binds α5, then α6 is incorporated, and at the end α7. In the absence of the chaperones Pba1-Pba2 or Ump1, alternative Pba4-containing complexes are detected, the formation of which depends on the Blm10/PA200 protein. Overexpression of Pba1-Pba2 abolishes the formation of these complexes containing Pba4 and Blm10, suggesting that Blm10 may replace Pba1-Pba2 as an alternative assembly factor.engProteasome core particleAssemblyChaperonesPba3-Pba4Blm10journal article10.3390/biom15050683