Nucleotide sequence of the head assembly gene cluster of bacteriophage L and decoration protein characterization

Nucleotide sequence of the head assembly gene cluster of bacteriophage L and decoration protein characterization
复制标题

DOI:
10.1128/jb.187.6.2050-2057.2005
复制
发表时间:
2005-03-01
影响因子:
3.2
通讯作者:
Casjens, SR
Casjens, SR
中科院分区:
生物学3区
文献类型:
--
作者:
Gilcrease, EB;Winn-Stapley, DA;Casjens, SR

文献摘要

被引文献

相似文献

温和沙门氏菌噬菌体L是研究非常充分的噬菌体P22的近亲。在这项研究中,我们表明,L原衣壳组装和DNA包装基因,编码末端酶,门户网站,支架,和外壳蛋白,是非常密切的亲属同源P22基因(96.3%至99.1%的编码氨基酸序列的同一性)。然而,我们也确定了一个L基因,dec,这是不存在于P22基因组中,并编码蛋白质(Dec),存在于表面上的L病毒粒子在约150至180分子/病毒粒子。我们还表明,Dec蛋白在溶液中是一个三聚体,它结合到P22病毒粒子的数量类似于L病毒粒子。它的结合显着稳定P22病毒粒子对破坏的镁离子螯合剂。Dec蛋白结合到P22外壳蛋白壳,该外壳蛋白壳在体内自然膨胀或通过十二烷基硫酸钠处理在体外膨胀,但不结合到未膨胀的原衣壳壳。最后,噬菌体L限制性位点的位置和一些补丁的核苷酸序列的分析表明,EST 64 T和L是非常密切的亲戚,也许是两个最近的亲戚,已独立分离到日期之间的EST 64。
The temperate Salmonella enterica bacteriophage L is a close relative of the very well studied bacteriophage P22. In this study we show that the L procapsid assembly and DNA packaging genes, which encode terminase, portal, scaffold, and coat proteins, are extremely close relatives of the homologous P22 genes (96.3 to 99.1% identity in encoded amino acid sequence). However, we also identify an L gene, dec, which is not present in the P22 genome and which encodes a protein (Dec) that is present on the surface of L virions in about 150 to 180 molecules/virion. We also show that the Dec protein is a trimer in solution and that it binds to P22 virions in numbers similar to those for L virions. Its binding dramatically stabilizes P22 virions against disruption by a magnesium ion chelating agent. Dec protein binds to P22 coat protein shells that have expanded naturally in vivo or by sodium dodecyl sulfate treatment in vitro but does not bind to unexpanded procapsid shells. Finally, analysis of phage L restriction site locations and a number of patches of nucleotide sequence suggest that phages ST64T and L are extremely close relatives, perhaps the two closest relatives that have been independently isolated to date among the lambdoid phages.