Expression and Properties of Bacteriophage T4 Gene Product 11

被引:0
作者
L. P. Kurochkina
P. G. Leiman
S. Yu. Venyaminov
V. V. Mesyanzhinov
机构
[1] Russian Academy of Sciences,Shemyakin and Ovchinnikov Institute of Bioorganic Chemistry
[2] Russian Academy of Sciences,Bach Institute of Biochemistry
[3] Mayo Foundation,Department of Biochemistry and Molecular Biology
[4] Russian Academy of Sciences,Shemyakin and Ovchinnikov Institute of Bioorganic Chemistry
来源
Biochemistry (Moscow) | 2001年 / 66卷
关键词
bacteriophage T4; baseplate; gene product 11; protein folding;
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摘要
A plasmid vector for expression of bacteriophage T4 gene product 11 (gp11) in E. coli cells has been constructed. Gp11 is a baseplate protein that connects short tail fibers providing irreversible adsorption of the virus on a cell. A method based on chromatography on hydroxyapatite has been developed for purification of recombinant gp11. The protein is active in an in vitro complementation assay and transforms defective phage particles lacking gp11 into infective ones. Gel filtration data suggest that the biologically active protein is a trimer. According to CD spectroscopy and sequence analysis data, the polypeptide chain of gp11 contains not less than 20% α-helical segments, about 30% β-structure, and belongs to the class of α/β structural proteins.
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页码:141 / 146
页数:5
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