Decelerated degradation of short peptides by the 20S proteasome

被引:52
作者
Dolenc, I
Seemüller, E
Baumeister, W
机构
[1] Max Planck Inst Biochem, D-82152 Martinsried, Germany
[2] Jozef Stefan Inst, Dept Biochem & Mol Biol, Ljubljana, Slovenia
关键词
proteasome; molecular ruler; protein degradation; Thermoplasma acidophilum;
D O I
10.1016/S0014-5793(98)01010-2
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
Based on a twelve residue master peptide comprising all five specific cleavage sites defined for the proteasome, a set of variant peptides was generated in order to probe specificity and to elucidate the mechanism which determines product size. It is shown that the rate of degradation by the 20S proteasome from Thermoplasma acidophilum depends critically on the length of the peptide substrate. Peptides of 14 residues and longer are degraded much faster than shorter peptides although the sites of cleavage remain unchanged. The decelerated degradation of peptides shorter than 14 residues explains the accumulation of products with an average length of seven to nine residues, (C) 1998 Federation of European Biochemical Societies.
引用
收藏
页码:357 / 361
页数:5
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