Dissecting the assembly pathway of the 20S proteasome
FEBS LettersPublished 24 November 1997Open access
Frank Zühl, Erika Seemüller, Ralph Golbik, Wolfgang Baumeister
Citations93
SJR quartileQ1
SJR score1.22
SNIP0.77
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TL;DR
Assembly studies with wild‐type and N‐terminally truncated β‐subunits in conjunction with refolding studies allowed to define the role of the propeptide which is two‐fold: It supports the initial folding of the β‐ subunits and it promotes the maturation of the holoproteasomes.
Abstract
Proteasomes reach their mature active state via a complex cascade of folding, assembly and processing events. The Rhodococcus proteasome offers a means to dissect the assembly pathway and to characterize intermediates; its four subunits (alpha1, alpha2, beta1, beta2) assemble efficiently in vitro with any combination of alpha and beta. Assembly studies with wild-type and N-terminally truncated beta-subunits in conjunction with refolding studies allowed to define the role of the propeptide which is two-fold: It supports the initial folding of the beta-subunits and it promotes the maturation of the holoproteasomes.
Keywords
MedicineBiochemistry, Genetics and Molecular Biology
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