The α5-α6-α7-Pba3-Pba4 Complex: A Starting Unit in Proteasome Core Particle Assembly

A 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 <i>Saccharomyces cerevisiae</i> cell<i>s</i>. 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.

Authors

Institutions

Publication Details

Journal
Biomolecules
Published
2025-05-08
DOI
https://doi.org/10.3390/biom15050683
Citations
3
Primary Topic
Ubiquitin and proteasome pathways
Type
article
Field-Weighted Citation Impact
2.42

Funders

Controls
|||
ALL TIME
JAN
FEB
MAR
APR
MAY
JUN
JUL
AUG
SEP
OCT
article

The α5-α6-α7-Pba3-Pba4 Complex: A Starting Unit in Proteasome Core Particle Assembly

Paula C. Ramos, Margarida N. Tiago, Ana Catarina Matias, R. Jürgen Dohmen et al.
3 citations
Biomolecules
Ubiquitin and proteasome pathways
2.42
article

The α5-α6-α7-Pba3-Pba4 Complex: A Starting Unit in Proteasome Core Particle Assembly

Paula C. Ramos, Margarida N. Tiago, Ana Catarina Matias, R. Jürgen Dohmen, Jessica Zimmermann
article en
3 citations

Abstract

A 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 <i>Saccharomyces cerevisiae</i> cell<i>s</i>. 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.

BiomoleculesVol. 15(5)
University of Cologne (DE), University of Algarve (PT)
Deutsche Forschungsgemeinschaft, Fundação para a Ciência e a Tecnologia
Life in Land
Openalex Percentile: Top 12%
Ubiquitin and proteasome pathways
2.42
AI Navigator

Ask Laika to Summarize, Analyze, and Connect papers live on the map.

Summarize Papers & Methodologies

Extract key findings, datasets, and comparative methods across publications.

Benchmark Rankings & Visual Analytics

Rank top research institutions, authors, funders, topics, and journals by Field-Weighted Citation Impact (FWCI) and paper volume with instant charts.

Connect Distant Disciplines

Bridge topological clusters on the map to find hidden collaborative intersections.

The α5-α6-α7-Pba3-Pba4 Complex: A Starting Unit in Proteasome Core Particle Assembly — Paula C. Ramos, Margarida N. Tiago, et al. · Biomolecules (2025) | TGRS Research Map | TGRS