Intrinsically unstructured regions in the C domain of the influenza virus M1 protein
Intrinsically unstructured regions in the C domain of the influenza virus M1 protein
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DOI：
10.1134/s0026893311030071
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发表时间：
2011-08-01
影响因子：
1.2
通讯作者：
Baratova, L. A.
中科院分区：
文献类型：
--
作者：
Ksenofontov, A. L.;Dobrov, E. N.;Baratova, L. A.
流感病毒的M1基质蛋白是病毒粒子的主要结构成分之一，在感染细胞中执行几种不同的功能。已对M1蛋白的N-末端部分（残基2-158）进行了X射线分析（分辨率为2.08），但未对其C-末端结构域（159-252）进行分析。在本研究中，我们分析了M1蛋白的流感病毒A/波多黎各/8/34（H1N1）株在酸性溶液中使用氚平面图的结构。氚标记的M1蛋白的结构域的掺入进行了研究; C结构域和域间环优先访问氚。分析离心和动态激光散射表明异常的流体动力学参数和低结构的M1蛋白，这也证实了圆二色性数据。M1蛋白质序列的生物信息学分析揭示了集中在C结构域和N-，M-和C结构域之间的域间环中的固有非结构化片段。我们认为，在细胞中的M1蛋白质的多功能性是由其三级结构的可塑性，这是由固有的非结构化片段的存在下所造成的。
The M1 matrix protein of the influenza virus is one of the main structural components of the virion that performs several different functions in the infected cell. X-ray analysis (with 2.08 resolution) has been performed for the N-terminal part of the M1 protein (residues 2-158) but not for its C-terminal domain (159-252). In the present study, we analyzed the structure of the M1 protein of the influenza virus A/Puerto Rico/8/34 (H1N1) strain in acidic solution using tritium planigraphy. The incorporation of tritium label into the domains of the M1 protein were studied; the C domain and the interdomain loops are preferentially accessible to tritium. Analytical centrifugation and dynamic laser light scattering demonstrated anomalous hydrodynamic parameters and low structuredness of the M1 protein, which has also been confirmed by circular dichroism data. Bioinformatic analysis of the M1 protein sequence revealed intrinsically unstructured segments that were concentrated in the C domain and interdomain loops between the N-, M-, and C domains. We suggest that the multifunctionality of the M1 protein in a cell is determined by the plasticity of its tertiary structure, which is caused by the presence of intrinsically unstructured segments.