Proteolytic processing of phage lambda tail protein gpH: timing of the cleavage.
Proteolytic processing of phage lambda tail protein gpH: timing of the cleavage.
复制标题
噬菌体 lambda 尾蛋白 gpH 的蛋白水解加工：切割时间。
DOI：
10.1016/0042-6822(83)90199-x
复制
发表时间：
1983
期刊：
影响因子：
3.7
通讯作者：
Hendrix,RW
中科院分区：
文献类型：
--
作者：
Tsui,LC;Hendrix,RW
我们描述了一种快速部分纯化噬菌体λ尾部组装中间结构的λ方法，使用甲醛固定的大肠杆菌细胞沉淀尾部相关结构。其净化依赖于三价体之间的特定相互作用。λ受体蛋白和λ尾蛋白gpJ。分析了尾部装配中间体的蛋白质组成，以确定在装配序列中次要尾部蛋白gpH被切割的时间。gpH在途径的早期，在引发剂（成为尾尖的结构）的组装过程中加入尾前体结构。然而，直到引发剂组装完成并在尾轴聚合到引发剂上之后，gpH才被劈裂。这些结果表明，每个gpH分子沿着尾巴的长度延伸。我们的结果似乎也消除了早期实验确定的尾部组装途径的模糊性：我们认为geneg在genesHandM之间起作用。
We describe λ method for the rapid partial purification of intermediate structures of phage λ tail assembly, using formaldehyde-fixedEscherichia colicells to precipitate tail-related structures. The purification depends on the specific interaction between theE. coliλ receptor protein and λ tail protein gpJ. Protein compositions of tail assembly intermediates were analyzed to determine when in the assembly sequence the minor tail protein gpH is cleaved. gpH joins the tail precursor structure early in the pathway, during assembly of the initiator (a structure that becomes the tail tip). However, gpH is not cleaved until after initiator assembly is complete and after the tail shaft has polymerized onto the initiator. These results suggest that each gpH molecule is extended along the length of the tail. Our results also appear to eliminate an ambiguity in the tail assembly pathway determined by earlier experiments: we argue that geneGacts between genesHandM.