In vitro dissection of the membrane and RNP binding activities of influenza virus M1 protein
In vitro dissection of the membrane and RNP binding activities of influenza virus M1 protein
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DOI：
10.1006/viro.2000.0804
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发表时间：
2001-03-01
期刊：
影响因子：
3.7
通讯作者：
Ruigrok, RWH
中科院分区：
文献类型：
--
作者：
Baudin, F;Petit, I;Ruigrok, RWH
流感病毒M1蛋白在结晶过程中的自发蛋白分解定义了1-164个氨基酸的N-末端结构域。体外实验表明，只有全长M1及其N-末端结构域与带负电荷的脂质体结合，只有全长M1及其C-末端部分与RNP结合。然而，只有全长M1具有转录抑制活性。几种独立的实验方法表明，在体外，转录抑制是通过M1聚合/聚集到RNP上，或者M1聚合/聚集到已经与RNP结合的M1上，而不是通过结合到核蛋白或聚合酶上的特定活性部位来发生的。流感病毒M1的结构/功能将与埃博拉病毒基质蛋白VP40进行比较。(C)2001年学术出版社。
Spontaneous proteolysis of influenza virus M1 protein during crystallisation has defined an N-terminal domain of amino acids 1-164. Full-length M1, the N-terminal domain, and the C-terminal part of M1 (residues 165-252) were produced in Escherichia coli in vitro tests showed that only full-length M1 and its N-terminal domain bind to negatively charged liposomes and that only full-length M1 and its C-terminal part bind to RNP. However, only full-length M1 had transcription inhibition activity. Several independent experimental approaches indicate that in vitro transcription inhibition occurs through polymerisation/aggregation of M1 onto RNP, or of M1 onto M1 already bound to RNP, rather than by binding to a specific active site on the nucleoprotein or the polymerase. The structure/function of influenza virus M1 will be compared with that of the Ebola virus matrix protein, VP40. (C) 2001 Academic Press.