Expression and properties of bacteriophage T4 gene product 11

L. P. Kurochkina; P. G. Leiman; S. Yu Venyaminov; V. V. Mesyanzhinov

doi:10.1023/A:1002831212462

Expression and properties of bacteriophage T4 gene product 11

L. P. Kurochkina, P. G. Leiman, S. Yu Venyaminov, V. V. Mesyanzhinov

Research output: Contribution to journal › Article › peer-review

4 Scopus citations

Abstract

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.

Original language	English (US)
Pages (from-to)	141-146
Number of pages	6
Journal	Biochemistry (Moscow)
Volume	66
Issue number	2
DOIs	https://doi.org/10.1023/A:1002831212462
State	Published - Feb 2001
Externally published	Yes

Keywords

Bacteriophage T4
Baseplate
Gene product 11
Protein folding

ASJC Scopus subject areas

Geriatrics and Gerontology
Biochemistry, Genetics and Molecular Biology (miscellaneous)
Biophysics
Biochemistry

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title = "Expression and properties of bacteriophage T4 gene product 11",

abstract = "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.",

keywords = "Bacteriophage T4, Baseplate, Gene product 11, Protein folding",

author = "Kurochkina, {L. P.} and Leiman, {P. G.} and Venyaminov, {S. Yu} and Mesyanzhinov, {V. V.}",

note = "Funding Information: This study was supported by grants from the Howard Hughes Medical Institute (No. 751952520803), the Russian Foundation for Basic Research (No. 992042 48430), and the “Universities of Russia” program (No. 26082415/98).",

year = "2001",

month = feb,

doi = "10.1023/A:1002831212462",

language = "English (US)",

volume = "66",

pages = "141--146",

journal = "Biochemistry (Moscow)",

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T1 - Expression and properties of bacteriophage T4 gene product 11

AU - Kurochkina, L. P.

AU - Leiman, P. G.

AU - Venyaminov, S. Yu

AU - Mesyanzhinov, V. V.

N1 - Funding Information: This study was supported by grants from the Howard Hughes Medical Institute (No. 751952520803), the Russian Foundation for Basic Research (No. 992042 48430), and the “Universities of Russia” program (No. 26082415/98).

PY - 2001/2

Y1 - 2001/2

N2 - 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.

AB - 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.

KW - Bacteriophage T4

KW - Baseplate

KW - Gene product 11

KW - Protein folding

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JO - Biochemistry (Moscow)

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IS - 2

ER -

Expression and properties of bacteriophage T4 gene product 11

Abstract

Keywords

ASJC Scopus subject areas

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