A model for nonstoichiometric, cotranslational protein scission in eukaryotic ribosomes
A model for nonstoichiometric, cotranslational protein scission in eukaryotic ribosomes
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DOI：
10.1006/bioo.1998.1119
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发表时间：
1999-02-01
影响因子：
5.1
通讯作者：
Gani, D
中科院分区：
文献类型：
--
作者：
Ryan, MD;Donnelly, M;Gani, D
口疮病毒2A区显然负责水解切割Gly-Pro键上的单个大多蛋白，只有18个氨基酸残基长，显然不是蛋白酶。在这里，我们描述了报告基因重组多聚蛋白的构建，并提供了进一步诱变实验的结果，旨在测试口蹄疫病毒（FMDV）2A区域内的特定氨基酸残基的功能。这些结果表明Gly-Pro酰胺键实际上没有合成。该结果可以合理化为一个动力学和结构模型的共翻译口疮和心脏病毒多蛋白裂解，其中水解是介导的核糖体结合的2A多肽-tRNA分子在其自己的3 '-O酰基腺苷酯键。的3-D结构的2A多肽在防止肽键的形成，但在允许的下游多肽序列的合成的可能作用进行了讨论的范围内的新的发现。(C)北京：科学出版社.
The aphthovirus 2A region apparently responsible for the hydrolytic cleavage of a single large polyprotein at a Gly-Pro linkage is only 18 amino acid residues long and is evidently not a proteinase. Here we describe the construction of reporter recombinant polyproteins and provide the results of further mutagenesis experiments designed to test the functions of specific amino acid residues within the foot-and-mouth disease virus (FMDV) 2A region. These results show that a Gly-Pro amide bond is not actually synthesized. The result can be rationalized into a kinetic and structural model for cotranslational aphtho- and cardiovirus polyprotein cleavage in which hydrolysis is mediated by a ribosomally bound 2A polypeptidyl-tRNA molecule at its own 3'-O acyl adenosyl ester linkage. The possible role of the 3-D structure of the 2A polypeptide in preventing peptide bond formation but in allowing the synthesis of the downstream polypeptide sequence is discussed within the context of the new findings. (C) 1999 Academic Press.