Gal repressosome contains an antiparallel DNA loop

Mark Geanacopoulos; George Vasmatzis; Victor B. Zhurkin; Sankar Adhya

doi:10.1038/87595

Gal repressosome contains an antiparallel DNA loop

Mark Geanacopoulos, George Vasmatzis, Victor B. Zhurkin, Sankar Adhya

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

80 Scopus citations

Abstract

Gal repressosome assembly and repression of the galoperon in Escherichia coil occurs when two dimeric GalR proteins and the histone-like HU protein bind to cognate sites causing DNA looping. Structure-based genetic analysis defined the GalR surfaces interacting to form a stacked, V-shaped, tetrameric structure. Stereochemical models of the four possible DNA loops compatible with the GalR tetramer configuration were constructed using the sequence-dependent structural parameters of the interoperator DNA and conformation changes caused by GalR and asymmetric HU binding. Evaluation of their DNA elastic energies gave unambiguous preference to a loop structure in which the two gal operators adopt an antiparallel orientation causing undertwisting of DNA.

Original language	English (US)
Pages (from-to)	432-436
Number of pages	5
Journal	Nature Structural Biology
Volume	8
Issue number	5
DOIs	https://doi.org/10.1038/87595
State	Published - 2001

ASJC Scopus subject areas

Structural Biology
Biochemistry
Genetics

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title = "Gal repressosome contains an antiparallel DNA loop",

abstract = "Gal repressosome assembly and repression of the galoperon in Escherichia coil occurs when two dimeric GalR proteins and the histone-like HU protein bind to cognate sites causing DNA looping. Structure-based genetic analysis defined the GalR surfaces interacting to form a stacked, V-shaped, tetrameric structure. Stereochemical models of the four possible DNA loops compatible with the GalR tetramer configuration were constructed using the sequence-dependent structural parameters of the interoperator DNA and conformation changes caused by GalR and asymmetric HU binding. Evaluation of their DNA elastic energies gave unambiguous preference to a loop structure in which the two gal operators adopt an antiparallel orientation causing undertwisting of DNA.",

author = "Mark Geanacopoulos and George Vasmatzis and Zhurkin, {Victor B.} and Sankar Adhya",

note = "Funding Information: We thank J. H{\"o}hfeld and R. Morimoto for plasmids expressing Bag-1M and Hsc70; A. Valencia and A. Buchberger for design and cloning of dnaK-K55A; T. Hesterkamp, A. Hoelz and T. Laufen for helpful discussions. This work was supported by grants of the DFG to J.R., and the DFG (Graduiertenkolleg Biochemie der Enzyme; Leibniz program) and the Fonds der Chemischen Industrie to B.B.",

year = "2001",

doi = "10.1038/87595",

language = "English (US)",

volume = "8",

pages = "432--436",

journal = "Nature Structural Biology",

issn = "1072-8368",

publisher = "Nature Publishing Group",

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T1 - Gal repressosome contains an antiparallel DNA loop

AU - Geanacopoulos, Mark

AU - Vasmatzis, George

AU - Zhurkin, Victor B.

AU - Adhya, Sankar

N1 - Funding Information: We thank J. Höhfeld and R. Morimoto for plasmids expressing Bag-1M and Hsc70; A. Valencia and A. Buchberger for design and cloning of dnaK-K55A; T. Hesterkamp, A. Hoelz and T. Laufen for helpful discussions. This work was supported by grants of the DFG to J.R., and the DFG (Graduiertenkolleg Biochemie der Enzyme; Leibniz program) and the Fonds der Chemischen Industrie to B.B.

PY - 2001

Y1 - 2001

N2 - Gal repressosome assembly and repression of the galoperon in Escherichia coil occurs when two dimeric GalR proteins and the histone-like HU protein bind to cognate sites causing DNA looping. Structure-based genetic analysis defined the GalR surfaces interacting to form a stacked, V-shaped, tetrameric structure. Stereochemical models of the four possible DNA loops compatible with the GalR tetramer configuration were constructed using the sequence-dependent structural parameters of the interoperator DNA and conformation changes caused by GalR and asymmetric HU binding. Evaluation of their DNA elastic energies gave unambiguous preference to a loop structure in which the two gal operators adopt an antiparallel orientation causing undertwisting of DNA.

AB - Gal repressosome assembly and repression of the galoperon in Escherichia coil occurs when two dimeric GalR proteins and the histone-like HU protein bind to cognate sites causing DNA looping. Structure-based genetic analysis defined the GalR surfaces interacting to form a stacked, V-shaped, tetrameric structure. Stereochemical models of the four possible DNA loops compatible with the GalR tetramer configuration were constructed using the sequence-dependent structural parameters of the interoperator DNA and conformation changes caused by GalR and asymmetric HU binding. Evaluation of their DNA elastic energies gave unambiguous preference to a loop structure in which the two gal operators adopt an antiparallel orientation causing undertwisting of DNA.

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DO - 10.1038/87595

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JF - Nature Structural Biology

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Gal repressosome contains an antiparallel DNA loop

Abstract

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