CONFORMATIONAL CONSTRAINTS IN PROTEIN-DEGRADATION BY THE 20S PROTEASOME

被引：177

作者：

WENZEL, T ^{[1
]}

BAUMEISTER, W ^{[1
]}

机构：

[1] MAX PLANCK INST BIOCHEM,D-82152 MARTINSRIED,GERMANY

来源：

NATURE STRUCTURAL BIOLOGY | 1995年 / 2卷 / 03期

关键词：

D O I：

10.1038/nsb0395-199

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

Conformationally stabilized peptides and unfolding intermediates of bovine alpha-lactalbumin have been used to define the degree of unfolding required for degradation by 20S proteasomes. It appears that complete unfolding and the absence of disulphide bonds are prerequisites for degradation, suggesting that a relatively narrow opening controls access to the inner proteolytic compartment of the barrel-shaped proteasome. This is corroborated by electron microscopy studies showing that the insulin B-chain, which is otherwise easily degraded, cannot pass the orifice of this putative peptide channel when a NanogoldTM particle with a diameter of similar to 2 nm is covalently attached to it.

引用

页码：199 / 204

页数：6

共 34 条

[1] EVIDENCE THAT THE NATURE OF AMINO-ACID-RESIDUES IN THE P-3 POSITION DIRECTS SUBSTRATES TO DISTINCT CATALYTIC SITES OF THE PITUITARY MULTICATALYTIC PROTEINASE COMPLEX (PROTEASOME) [J].