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首页> 外文期刊>Journal of Molecular Biology >Sequence signals for generation of antigenic peptides by the proteasome: implications for proteasomal cleavage mechanism.
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Sequence signals for generation of antigenic peptides by the proteasome: implications for proteasomal cleavage mechanism.

机译：蛋白酶体产生抗原肽的序列信号：对蛋白酶体切割机制的影响。

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摘要

Proteasomal cleavage of proteins is the first step in the processing of most antigenic peptides that are presented to cytotoxic T cells. Still, its specificity and mechanism are not fully understood. To identify preferred sequence signals that are used for generation of antigenic peptides by the proteasome, we performed a rigorous analysis of the residues at the termini and flanking regions of naturally processed peptides eluted from MHC class I molecules. Our results show that both the C terminus (position P1 of the cleavage site) and its immediate flanking position (P1') possess significant signals. The N termini of the peptides show these signals only weakly, consistent with previous findings that antigenic peptides may be cleaved by the proteasome with N-terminal extensions. Nevertheless, we succeed to demonstrate indirectly that the N-terminal cleavage sites contain the same preferred signals at position P1'. This reinforces previous findings regarding the role of the P1' position of a cleavage site in determining the cleavage specificity, in addition to the well-known contribution of position P1. Our results apply to the generation of antigenic peptides and bare direct implications for the mechanism of proteasomal cleavage. We propose a model for proteasomal cleavage mechanism by which both ends of cleaved fragments are determined by the same cleavage signals, involving preferred residues at both P1 and P1' positions of a cleavage site. The compatibility of this model with experimental data on protein degradation products and generation of antigenic peptides is demonstrated. Copyright 2000 Academic Press.
机译：蛋白酶体切割蛋白质是加工呈现给细胞毒性T细胞的大多数抗原性肽的第一步。仍然，其特异性和机制尚未完全了解。为了鉴定蛋白酶体用于生成抗原肽的优选序列信号，我们对从I类MHC分子洗脱的天然加工肽的末端和侧翼区域的残基进行了严格分析。我们的结果表明，C末端（切割位点的位置P1）及其直接侧翼位置（P1'）均具有重要信号。肽的N末端仅微弱地显示这些信号，这与以前的发现一致，即抗原肽可以被具有N端延伸的蛋白酶切割。然而，我们成功地间接证明了N末端切割位点在位置P1'处包含相同的优选信号。除了位置P1的众所周知的贡献之外，这还增强了先前关于切割位点的P1'位置在确定切割特异性中的作用的发现。我们的结果适用于抗原肽的产生，对蛋白酶体切割的机制几乎没有直接影响。我们提出了蛋白酶体切割机制的模型，通过该模型，切割片段的两端由相同的切割信号确定，涉及切割位点的P1和P1'位置的优选残基。证明了该模型与蛋白质降解产物和抗原肽生成的实验数据的兼容性。版权所有2000学术出版社。

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