CAPSID PROTEIN VP4 OF POLIOVIRUS IS N-MYRISTOYLATED
CAPSID PROTEIN VP4 OF POLIOVIRUS IS N-MYRISTOYLATED
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DOI：
10.1073/pnas.84.22.7827
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发表时间：
1987-11-01
影响因子：
11.1
通讯作者：
WIMMER, E
中科院分区：
文献类型：
--
作者：
PAUL, AV;SCHULTZ, A;WIMMER, E
用[3 H]肉豆蔻酸在体内标记脊髓灰质炎病毒。衣壳多肽的分析显示，[3 H]肉豆蔻酸残基与病毒粒子的最小和内部衣壳蛋白VP 4共纯化。证据表明，明确的N-末端甘氨酸残基的VP 4是N-豆蔻酰化。先前对VP 4的胰蛋白酶肽的分析[Dorner，A. J.，多纳湖F.、拉森湾R.，维默，E.和安德森，C. W.（1982）J. Virol. 42，1017-1028]已经表明N-末端封闭基团存在于所有VP 4分子上以及VP 0和P1上，这是脊髓灰质炎病毒中VP 4的两种前体多肽。讨论了VP 4及其前体中肉豆蔻酸残基在脊髓灰质炎病毒增殖中的可能功能。
Poliovirus was labeled in vivo with [3H]myristic acid. Analysis of the capsid polypeptides revealed that the [3H]myristic acid residues copurified with VP4, the smallest and internal capsid protein of the virion. Evidence is presented showing unambiguously that the N-terminal glycine residue of VP4 is N-myristoylated. A previous analysis of the tryptic peptides of VP4 [Dorner, A. J., Dorner, L. F., Larsen, G. R., Wimmer, E. and Anderson, C. W. (1982) J. Virol. 42, 1017-1028] had shown that the N-terminal blocking group exists on all VP4 molecules as well as on VP0 and P1, two precursor polypeptides to VP4 in poliovirus. The possible function of the myristic acid residue in VP4 and in its precursor in poliovirus proliferation is discussed.