Observation of unexpected molecular binding activity for Mu phage tail fiber chaperones.
Observation of unexpected molecular binding activity for Mu phage tail fiber chaperones.
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DOI:
10.1093/jb/mvz068
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发表时间:
2019-12
影响因子:
2.7
通讯作者:
K. Sakai;T. Iwazaki;E. Yamashita;A. Nakagawa;Fumiya Sakuraba;Atsushi Enomoto;M. Inagaki;S. Takeda
中科院分区:
文献类型:
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作者:
K. Sakai;T. Iwazaki;E. Yamashita;A. Nakagawa;Fumiya Sakuraba;Atsushi Enomoto;M. Inagaki;S. Takeda
In the history of viral research, one of the important biological features of bacteriophage Mu is the ability to expand its host range. For extending host range, the Mu phage encodes two alternate tail fiber genes. Classical amber mutation experiments and genome sequence analysis of Mu phage suggested that gene products (gp) of geneS (gpS = gp49) and gene S' (gpS' = gp52) are tail fibers and that gene products of geneU (gpU = gp50) and geneU' (gpU' = gp51) work for tail fiber assembly or tail fiber chaperones. Depending on the gene orientation, a pair of genes 49 - 50 or 52 - 51 is expressed for producing different tail fibers that enable Mu phage to recognize different host cell surface. Since several fibrous proteins including some phage tail fibers employ their specific chaperone to facilitate folding and prevent aggregation, we expected that gp50 or gp51 would be a specific chaperone for gp49 and gp52, respectively. However, heterologous overexpression results for gp49 or gp52 (tail fiber subunit) together with gp51 and gp50, respectively, were also effective in producing soluble Mu tail fibers. Moreover, we successfully purified non-native gp49-gp51 and gp52-gp50 complexes. These facts showed that gp50 and gp51 was fungible and functional for both gp49 and gp52 each other.