期刊论文详细信息
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.
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【 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   

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