Hsp70 and Hsp110 chaperones promote early steps of proteasome assembly

• Autor(a) principal: A. C., Matias
• Data de Publicação: 2022
• Outros Autores: Matos, Joao, Dohmen, R. Jürgen, Ramos, Paula C.
• Tipo de documento: Artigo
• Idioma: eng
• Título da fonte: Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos)
• Texto Completo: http://hdl.handle.net/10400.1/19133
• topic: Proteasome biogenesis; Chaperones; Hsp70; Hsp110; Ssa1; Sse1

Whereas assembly of the 20S proteasome core particle (CP) in prokaryotes apparently occurs spontaneously, the efficiency of this process in eukaryotes relies on the dedicated assembly chaperones Ump1, Pba1-Pba2, and Pba3-Pba4. For mammals, it was reported that CP assembly initiates with formation of a complete alpha-ring that functions as a template for beta subunit incorporation. By contrast, we were not able to detect a ring composed only of a complete set of alpha subunits in S. cerevisiae. Instead, we found that the CP subunits alpha 1, alpha 2, and alpha 4 each form independent small complexes. Purification of such complexes containing alpha 4 revealed the presence of chaperones of the Hsp70/Ssa and Hsp110/Sse families. Consistently, certain small complexes containing alpha 1, alpha 2, and alpha 4 were not formed in strains lacking these chaperones. Deletion of the SSE1 gene in combination with deletions of PRE9 (alpha 3), PBA3, or UMP1 genes resulted in severe synthetic growth defects, high levels of ubiquitin-conjugates, and an accumulation of distinct small complexes with alpha subunits. Our study shows that Hsp70 and Hsp110 chaperones cooperate to promote the folding of individual alpha subunits and/or their assembly with other CP subunits, Ump1, and Pba1-Pba4 in subsequent steps.