Dolenc I, Seemüller E, Baumeister W
Max-Planck-Institut fur Biochemie, Martinsried, Germany.
FEBS Lett. 1998 Sep 4;434(3):357-61. doi: 10.1016/s0014-5793(98)01010-2.
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.
基于一个包含为蛋白酶体定义的所有五个特定切割位点的十二肽主肽，生成了一组变体肽，以探究特异性并阐明决定产物大小的机制。结果表明，嗜热栖热菌20S蛋白酶体的降解速率关键取决于肽底物的长度。14个及以上残基的肽比短肽降解得快得多，尽管切割位点保持不变。短于14个残基的肽降解减速解释了平均长度为7至9个残基的产物的积累。
