Stoltze L, Schirle M, Schwarz G, Schröter C, Thompson M W, Hersh L B, Kalbacher H, Stevanovic S, Rammensee H G, Schild H
Institute for Cell Biology, Department of Immunology, University of Tübingen, Auf der Morgenstelle 15, D-72076 Tübingen, Germany.
Nat Immunol. 2000 Nov;1(5):413-8. doi: 10.1038/80852.
The proteasome generates exact major histocompatibility complex (MHC) class I ligands as well as NH2-terminal-extended precursor peptides. The proteases responsible for the final NH2-terminal trimming of the precursor peptides had, until now, not been determined. By using specific selective criteria we purified two cytosolic proteolytic activities, puromycin-sensitive aminopeptidase and bleomycin hydrolase. These proteases could remove NH2-terminal amino acids from the vesicular stomatitis virus nucleoprotein cytotoxic T cell epitope 52-59 (RGYVYQGL) resulting, in combination with proteasomes, in the generation of the correct epitope. Our data provide evidence for the existence of redundant systems acting downstream of the proteasome in the antigen-processing pathway for MHC class I molecules.
蛋白酶体产生精确的主要组织相容性复合体（MHC）I类配体以及氨基末端延伸的前体肽。迄今为止，负责前体肽最终氨基末端修剪的蛋白酶尚未确定。通过使用特定的选择标准，我们纯化了两种胞质蛋白水解活性，即嘌呤霉素敏感的氨肽酶和博来霉素水解酶。这些蛋白酶可以从水疱性口炎病毒核蛋白细胞毒性T细胞表位52 - 59（RGYVYQGL）中去除氨基末端氨基酸，与蛋白酶体共同作用产生正确的表位。我们的数据为在MHC I类分子抗原加工途径中蛋白酶体下游存在冗余系统提供了证据。
