当前位置: X-MOL 学术J. Mol. Biol. › 论文详情
Our official English website, www.x-mol.net, welcomes your feedback! (Note: you will need to create a separate account there.)
Phage G Structure at 6.1 Å Resolution, Condensed DNA, and Host Identity Revision to a Lysinibacillus.
Journal of Molecular Biology ( IF 5.6 ) Pub Date : 2020-05-23 , DOI: 10.1016/j.jmb.2020.05.016
Brenda González 1 , Lyman Monroe 1 , Kunpeng Li 1 , Rui Yan 1 , Elena Wright 2 , Thomas Walter 1 , Daisuke Kihara 3 , Susan T Weintraub 2 , Julie A Thomas 4 , Philip Serwer 2 , Wen Jiang 5
Affiliation  

Phage G has the largest capsid and genome of any known propagated phage. Many aspects of its structure, assembly, and replication have not been elucidated. Herein, we present the dsDNA-packed and empty phage G capsid at 6.1 and 9 Å resolution, respectively, using cryo-EM for structure determination and mass spectrometry for protein identification. The major capsid protein, gp27, is identified and found to share the HK97-fold universally conserved in all previously solved dsDNA phages. Trimers of the decoration protein, gp26, sit on the 3-fold axes and are thought to enhance the interactions of the hexameric capsomeres of gp27, for other phages encoding decoration proteins. Phage G's decoration protein is longer than what has been reported in other phages, and we suspect the extra interaction surface area helps stabilize the capsid. We identified several additional capsid proteins, including a candidate for the prohead protease responsible for processing gp27. Furthermore, cryo-EM reveals a range of partially full, condensed DNA densities that appear to have no contact with capsid shell. Three analyses confirm that the phage G host is a Lysinibacillus, and not Bacillus megaterium: identity of host proteins in our mass spectrometry analyses, genome sequence of the phage G host, and host range of phage G.



中文翻译:

6.1Å分辨率的噬菌体G结构,浓缩的DNA以及对Lysinibacillus的宿主身份的修改。

噬菌体G具有任何已知繁殖噬菌体中最大的衣壳和基因组。其结构,组装和复制的许多方面尚未阐明。在这里,我们提出了dsDNA的包装和空噬菌体G衣壳分别在6.1和9Å的分辨率,使用cryo-EM进行结构确定和质谱法进行蛋白质鉴定。鉴定出主要衣壳蛋白gp27,发现其与所有先前解析的dsDNA噬菌体具有普遍保守的HK97倍。装饰蛋白的三聚体gp26位于3轴上,对于编码装饰蛋白的其他噬菌体,它们被认为可以增强gp27六聚体体的相互作用。噬菌体G的修饰蛋白比其他噬菌体中报道的蛋白长,我们怀疑额外的相互作用表面积有助于稳定衣壳。我们确定了几个其他衣壳蛋白,包括负责处理gp27的前额蛋白酶的候选人。此外,cryo-EM揭示了一系列部分充满的,浓缩的DNA密度,这些密度似乎与衣壳没有接触。三种分析证实噬菌体G宿主是一种溶菌杆菌而非巨大芽孢杆菌:在我们的质谱分析中宿主蛋白的身份,噬菌体G宿主的基因组序列以及噬菌体G的宿主范围。

更新日期:2020-06-23
down
wechat
bug