病毒组装过程中的蛋白质切割：噬菌体T4中依赖组装的切割的新特异性。
Protein cleavage during virus assembly: a novel specificity of assembly dependent cleavage in bacteriophage T4.
作者信息
Isobe T, Black L W, Tsugita A
出版信息
Proc Natl Acad Sci U S A. 1976 Nov;73(11):4205-9. doi: 10.1073/pnas.73.11.4205.
Abstract
Cleavage of precursor proteins occurs during assembly of numerous viruses. Seven bacteriophage T4 head-related proteins areknown to be cleaved during morphogenesis. Sequences surrounding the cleavage sites in T4 head precursors P23 and IPIII are reported here. We previously determined the sequences of precursor and processed forms of IPII and IPI. Cleavage occurs at a glutamyl-alanyl bond in each protein. By comparison of sequences around five cleaved and four uncleaved Glu-Ala bonds in head precursors, it appears that cleavage is limited to the Thr or Ala, and X2 to hydrophilic residues. The results suggest the viral-induced assembly protease recognizes and cleaves an extended primary structure in the structurally dissimilar precursors.
摘要
前体蛋白的切割发生在众多病毒的组装过程中。已知七种噬菌体T4头部相关蛋白在形态发生过程中会被切割。本文报道了T4头部前体P23和IPIII中切割位点周围的序列。我们之前已经确定了IPII和IPI的前体和加工形式的序列。每种蛋白的切割都发生在谷氨酰-丙氨酰键处。通过比较头部前体中五个已切割和四个未切割的Glu-Ala键周围的序列，似乎切割仅限于苏氨酸或丙氨酸，且X2为亲水残基。结果表明，病毒诱导的组装蛋白酶识别并切割结构不同的前体中的延伸一级结构。
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