蛋白酶体抑制剂PI31与PA28竞争结合20S蛋白酶体。

The proteasome inhibitor PI31 competes with PA28 for binding to 20S proteasomes.

作者信息

Zaiss D M, Standera S, Holzhütter H, Kloetzel P, Sijts A J

机构信息

Institute of Biochemistry/Charité, Monbijou Strasse 2, D-10117, Berlin, Germany.

出版信息

FEBS Lett. 1999 Sep 3;457(3):333-8. doi: 10.1016/s0014-5793(99)01072-8.

DOI:10.1016/s0014-5793(99)01072-8

PMID:10471803

Abstract

PI31 is a previously described inhibitor of 20S proteasomes. Using recombinant PI31 we have analyzed its effect on proteasomal hydrolyzing activity of short fluorogenic substrates and of a synthetic 40-mer polypeptide. In addition, we investigated its influence on the activation of 20S proteasome by the proteasome activator PA28. PI31 inhibits polypeptide degradation already at concentrations which only partially inhibit fluorogenic substrate turnover and immunosubunits do not influence the PI31 binding affinity. Furthermore our data demonstrate that PI31 is a potent competitor of PA28-mediated activation.

摘要

PI31是一种先前已被描述的20S蛋白酶体抑制剂。我们使用重组PI31分析了其对短荧光底物和合成的40聚体多肽的蛋白酶体水解活性的影响。此外，我们研究了其对蛋白酶体激活剂PA28激活20S蛋白酶体的影响。PI31在仅部分抑制荧光底物周转的浓度下就已抑制多肽降解，且免疫亚基不影响PI31的结合亲和力。此外，我们的数据表明PI31是PA28介导的激活的有效竞争者。