A Novel Indirect Sequence Readout Component in the E. coli Cyclic AMP Receptor Protein Operator

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Standard

A Novel Indirect Sequence Readout Component in the E. coli Cyclic AMP Receptor Protein Operator. / Lindemose, Søren; Nielsen, Peter Eigil; Valentin-Hansen, Poul; Møllegaard, Niels Erik.

I: ACS chemical biology, Bind 9, Nr. 3, 21.03.2014, s. 752-60.

Publikation: Bidrag til tidsskrift › Tidsskriftartikel › Forskning › fagfællebedømt

Harvard

Lindemose, S, Nielsen, PE, Valentin-Hansen, P & Møllegaard, NE 2014, 'A Novel Indirect Sequence Readout Component in the E. coli Cyclic AMP Receptor Protein Operator', ACS chemical biology, bind 9, nr. 3, s. 752-60. https://doi.org/10.1021/cb4008309

APA

Lindemose, S., Nielsen, P. E., Valentin-Hansen, P., & Møllegaard, N. E. (2014). A Novel Indirect Sequence Readout Component in the E. coli Cyclic AMP Receptor Protein Operator. ACS chemical biology, 9(3), 752-60. https://doi.org/10.1021/cb4008309

Vancouver

Lindemose S, Nielsen PE, Valentin-Hansen P, Møllegaard NE. A Novel Indirect Sequence Readout Component in the E. coli Cyclic AMP Receptor Protein Operator. ACS chemical biology. 2014 mar. 21;9(3):752-60. https://doi.org/10.1021/cb4008309

Author

Lindemose, Søren ; Nielsen, Peter Eigil ; Valentin-Hansen, Poul ; Møllegaard, Niels Erik. / A Novel Indirect Sequence Readout Component in the E. coli Cyclic AMP Receptor Protein Operator. I: ACS chemical biology. 2014 ; Bind 9, Nr. 3. s. 752-60.

Bibtex

@article{c6c12c51843a40aab45e7aaa342c6504,
title = "A Novel Indirect Sequence Readout Component in the E. coli Cyclic AMP Receptor Protein Operator",
abstract = "The cyclic AMP receptor protein (CRP) from Escherichia coli has been extensively studied for several decades. In particular, a detailed characterization of CRP interaction with DNA has been obtained. The CRP dimer recognizes a consensus sequence AANTGTGANNNNNNTCACANTT through direct amino acid nucleobase interactions in the major groove of the two operator half-sites. Crystal structure analyses have revealed that the interaction results in two strong kinks at the TG/CA steps closest to the 6-base-pair spacer (N6). This spacer exhibits high sequence variability among the more than 100 natural binding sites in the E. coli genome, but the exact role of the N6 region in CRP interaction has not previously been systematic examined. Here we employ an in vitro selection system based on a randomized N6 spacer region to demonstrate that CRP binding to the lacP1 site may be enhanced up to 14-fold or abolished by varying the N6 spacer sequences. Furthermore, on the basis of sequence analysis and uranyl (UO2(2+)) probing data, we propose that the underlying mechanism relies on N6 deformability.",
author = "S{\o}ren Lindemose and Nielsen, {Peter Eigil} and Poul Valentin-Hansen and M{\o}llegaard, {Niels Erik}",
year = "2014",
month = mar,
day = "21",
doi = "10.1021/cb4008309",
language = "English",
volume = "9",
pages = "752--60",
journal = "A C S Chemical Biology",
issn = "1554-8929",
publisher = "American Chemical Society",
number = "3",

}

RIS

TY - JOUR

T1 - A Novel Indirect Sequence Readout Component in the E. coli Cyclic AMP Receptor Protein Operator

AU - Lindemose, Søren

AU - Nielsen, Peter Eigil

AU - Valentin-Hansen, Poul

AU - Møllegaard, Niels Erik

PY - 2014/3/21

Y1 - 2014/3/21

N2 - The cyclic AMP receptor protein (CRP) from Escherichia coli has been extensively studied for several decades. In particular, a detailed characterization of CRP interaction with DNA has been obtained. The CRP dimer recognizes a consensus sequence AANTGTGANNNNNNTCACANTT through direct amino acid nucleobase interactions in the major groove of the two operator half-sites. Crystal structure analyses have revealed that the interaction results in two strong kinks at the TG/CA steps closest to the 6-base-pair spacer (N6). This spacer exhibits high sequence variability among the more than 100 natural binding sites in the E. coli genome, but the exact role of the N6 region in CRP interaction has not previously been systematic examined. Here we employ an in vitro selection system based on a randomized N6 spacer region to demonstrate that CRP binding to the lacP1 site may be enhanced up to 14-fold or abolished by varying the N6 spacer sequences. Furthermore, on the basis of sequence analysis and uranyl (UO2(2+)) probing data, we propose that the underlying mechanism relies on N6 deformability.

AB - The cyclic AMP receptor protein (CRP) from Escherichia coli has been extensively studied for several decades. In particular, a detailed characterization of CRP interaction with DNA has been obtained. The CRP dimer recognizes a consensus sequence AANTGTGANNNNNNTCACANTT through direct amino acid nucleobase interactions in the major groove of the two operator half-sites. Crystal structure analyses have revealed that the interaction results in two strong kinks at the TG/CA steps closest to the 6-base-pair spacer (N6). This spacer exhibits high sequence variability among the more than 100 natural binding sites in the E. coli genome, but the exact role of the N6 region in CRP interaction has not previously been systematic examined. Here we employ an in vitro selection system based on a randomized N6 spacer region to demonstrate that CRP binding to the lacP1 site may be enhanced up to 14-fold or abolished by varying the N6 spacer sequences. Furthermore, on the basis of sequence analysis and uranyl (UO2(2+)) probing data, we propose that the underlying mechanism relies on N6 deformability.

U2 - 10.1021/cb4008309

DO - 10.1021/cb4008309

M3 - Journal article

C2 - 24387622

VL - 9

SP - 752

EP - 760

JO - A C S Chemical Biology

JF - A C S Chemical Biology

SN - 1554-8929

IS - 3

ER -

ID: 108770000