Membrane relocation but not tight binding of human immunodeficiency virus type 1 Gag particles myristoylated in Escherichia coli.

Membrane relocation but not tight binding of human immunodeficiency virus type 1 Gag particles myristoylated in Escherichia coli.
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大肠杆菌中肉豆蔻酰化的人类免疫缺陷病毒 1 型 Gag 颗粒的膜重新定位但不紧密结合。

DOI:
10.1006/viro.2001.0886
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发表时间:
2001
期刊:
影响因子:
3.7
通讯作者:
K. Sano
K. Sano
中科院分区:
医学3区
文献类型:
--
作者:
Y. Morikawa;A. Kinoshita;T. Goto;H. Tomoda;K. Sano

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Expression of human immunodeficiency virus Gag protein and the N-terminal matrix (MA) domain in Escherichia coli yielded spherical structures in the cytoplasm. When human N-myristoyltransferase was coexpressed, both Gag and MA were fully myristoylated and spherical structures were relocated in close proximity to the cytoplasmic membrane. However, neither myristoylated Gag nor MA exhibited tight binding to E. coli membrane, suggesting that myristoylation in E. coli did not confer membrane affinity on Gag despite the relocation. Our data also suggest that the morphogenetic pathway of Gag particles in prokaryotic cells differs from that in eukaryotic cells despite biochemical similarities of in the form of Gag expressed.
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