FEBS Letters | |
Dissecting the assembly pathway of the 20S proteasome | |
Baumeister, Wolfgang2  Seemüller, Erika2  Golbik, Ralph1  Zühl, Frank2  | |
[1] Martin Luther University Halle-Wittenberg, D-06120 Halle, Germany;Max-Planck-Institute for Biochemistry, D-82152 Martinsried, Germany | |
关键词: Proteasome; Rhodococcus; Processing; Assembly; Propeptide; SDS; sodium dodecyl sulfate; PAGE; polyacrylamide gel electrophoresis; AMC; 7-amino-4-methylcoumarin; Suc; succinyl; pre; precursor; pro; propeptide; βΔ; β-subunit with propeptide deleted; | |
DOI : 10.1016/S0014-5793(97)01370-7 | |
学科分类:生物化学/生物物理 | |
来源: John Wiley & Sons Ltd. | |
【 摘 要 】
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 (α1, α2, β1, β2) assemble efficiently in vitro with any combination of α and β. 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.
【 授权许可】
Unknown
【 预 览 】
Files | Size | Format | View |
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RO201912020305258ZK.pdf | 837KB | download |