Nucleocapsid protein structures from orthobunyaviruses reveal insight into ribonucleoprotein architecture and RNA polymerization.
Nucleocapsid protein structures from orthobunyaviruses reveal insight into ribonucleoprotein architecture and RNA polymerization.
复制标题
DOI：
10.1093/nar/gkt268
复制
发表时间：
2013-06
影响因子：
14.9
通讯作者：
Edwards TA
中科院分区：
文献类型：
--
作者：
Ariza A;Tanner SJ;Walter CT;Dent KC;Shepherd DA;Wu W;Matthews SV;Hiscox JA;Green TJ;Luo M;Elliott RM;Fooks AR;Ashcroft AE;Stonehouse NJ;Ranson NA;Barr JN;Edwards TA
所有正布尼亚病毒都具有三个单链负义RNA的基因组片段，其与病毒编码的核衣壳（N）蛋白结合以形成核糖核蛋白（RNP）复合物，其在高分辨率下未表征。我们报告的晶体结构的布尼亚韦拉病毒（BUNV）的N-RNA复合物和未结合的施马伦贝格病毒（SBV）N蛋白，分辨率分别为3.20和2.75 μ m。这两种N蛋白结晶为环状四聚体，并表现出高度的结构相似性，尽管分为不同的正布尼亚病毒血清组。这些结构代表了一种新的RNA结合蛋白折叠。BUNV N具有带正电荷的凹槽，RNA被深深地隔离在其中，碱基背对溶剂。这个位置是非常难以接近的，这意味着RNA聚合和病毒生命周期中的其他关键碱基配对事件需要RNP拆卸。N蛋白的突变分析支持结构和功能之间的相关性。这些晶体结构和电子显微镜图像的可溶性四聚体和真实的RNP之间的比较表明，N蛋白不结合RNA作为一个重复的单体，因此，它代表了一个新描述的架构布尼亚病毒RNP组装，与许多其他分段负链RNA病毒的影响。
All orthobunyaviruses possess three genome segments of single-stranded negative sense RNA that are encapsidated with the virus-encoded nucleocapsid (N) protein to form a ribonucleoprotein (RNP) complex, which is uncharacterized at high resolution. We report the crystal structure of both the Bunyamwera virus (BUNV) N–RNA complex and the unbound Schmallenberg virus (SBV) N protein, at resolutions of 3.20 and 2.75 Å, respectively. Both N proteins crystallized as ring-like tetramers and exhibit a high degree of structural similarity despite classification into different orthobunyavirus serogroups. The structures represent a new RNA-binding protein fold. BUNV N possesses a positively charged groove into which RNA is deeply sequestered, with the bases facing away from the solvent. This location is highly inaccessible, implying that RNA polymerization and other critical base pairing events in the virus life cycle require RNP disassembly. Mutational analysis of N protein supports a correlation between structure and function. Comparison between these crystal structures and electron microscopy images of both soluble tetramers and authentic RNPs suggests the N protein does not bind RNA as a repeating monomer; thus, it represents a newly described architecture for bunyavirus RNP assembly, with implications for many other segmented negative-strand RNA viruses.
登录
查看更多内容
影响因子：
11.8
作者：
Goller KV;Höper D;Schirrmeier H;Mettenleiter TC;Beer M
通讯作者：
Beer M
影响因子：
5.4
作者：
GARCIN, D;LEZZI, M;KOLAKOFSKY, D
通讯作者：
KOLAKOFSKY, D
DOI：
10.1107/s0907444905036693
发表时间：
2006-01-01
影响因子：
2.2
作者：
Evans, P
通讯作者：
Evans, P
DOI：
10.1107/s0907444904019158
发表时间：
2004-12-01
影响因子：
2.2
作者：
Emsley, P;Cowtan, K
通讯作者：
Cowtan, K
影响因子：
5.4
作者：
Carter, Stephen D.;Surtees, Rebecca;Barr, John N.
通讯作者：
Barr, John N.