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Characterization of the interaction between topoisomerase II and DNA by transcriptional footprinting

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Standard

Characterization of the interaction between topoisomerase II and DNA by transcriptional footprinting. / Thomsen, B; Bendixen, C; Lund, K et al.

In: Journal of Molecular Biology, Vol. 215, No. 2, 20.09.1990, p. 237-44.

Research output: Contribution to journal/Conference contribution in journal/Contribution to newspaper › Journal article › Research › peer-review

Harvard

Thomsen, B, Bendixen, C, Lund, K, Andersen, AH, Sørensen, BS & Westergaard, O 1990, 'Characterization of the interaction between topoisomerase II and DNA by transcriptional footprinting', Journal of Molecular Biology, vol. 215, no. 2, pp. 237-44. https://doi.org/10.1016/S0022-2836(05)80342-0

APA

Thomsen, B., Bendixen, C., Lund, K., Andersen, A. H., Sørensen, B. S., & Westergaard, O. (1990). Characterization of the interaction between topoisomerase II and DNA by transcriptional footprinting. Journal of Molecular Biology, 215(2), 237-44. https://doi.org/10.1016/S0022-2836(05)80342-0

CBE

Thomsen B, Bendixen C, Lund K, Andersen AH, Sørensen BS, Westergaard O. 1990. Characterization of the interaction between topoisomerase II and DNA by transcriptional footprinting. Journal of Molecular Biology. 215(2):237-44. https://doi.org/10.1016/S0022-2836(05)80342-0

MLA

Thomsen, B et al. "Characterization of the interaction between topoisomerase II and DNA by transcriptional footprinting". Journal of Molecular Biology. 1990, 215(2). 237-44. https://doi.org/10.1016/S0022-2836(05)80342-0

Vancouver

Thomsen B, Bendixen C, Lund K, Andersen AH, Sørensen BS, Westergaard O. Characterization of the interaction between topoisomerase II and DNA by transcriptional footprinting. Journal of Molecular Biology. 1990 Sept 20;215(2):237-44. doi: 10.1016/S0022-2836(05)80342-0

Author

Thomsen, B ; Bendixen, C ; Lund, K et al. / Characterization of the interaction between topoisomerase II and DNA by transcriptional footprinting. In: Journal of Molecular Biology. 1990 ; Vol. 215, No. 2. pp. 237-44.

Bibtex

@article{5ed951c5061f4e8ab374e09320206a48,
title = "Characterization of the interaction between topoisomerase II and DNA by transcriptional footprinting",
abstract = "The interaction between calf thymus topoisomerase II and DNA has been characterized using a transcription assay. A highly preferred recognition sequence for topoisomerase II was inserted in either direction downstream from a promoter specific for a bacteriophage RNA polymerase. The presence of topoisomerase II-DNA complexes on the template provoked blockage of transcription, yielding RNA transcripts terminated 5' to the topoisomerase II binding site. A footprint of topoisomerase II, derived from transcription towards the complex from either side, revealed that eukaryotic topoisomerase II binds a region of 28 base-pairs with a highly protected central core of 22 base-pairs. The binding region was located symmetrically around the topoisomerase II-mediated cleavage site. In agreement with this result, optimal topoisomerase II-mediated cleavage was observed with a DNA substrate consisting of a 28-mer oligonucleotide homologous to the protected region. Stepwise removal of base-pairs from the ends of the 28-mer gradually reduced the level of enzyme-mediated cleavage.",
keywords = "Acetanilides, Animals, Base Sequence, Binding Sites, Cattle, DNA, DNA Topoisomerases, Type I, DNA-Binding Proteins, In Vitro Techniques, Molecular Sequence Data, Nitroimidazoles, Transcription, Genetic, Journal Article, Research Support, Non-U.S. Gov't",
author = "B Thomsen and C Bendixen and K Lund and Andersen, {A H} and S{\o}rensen, {B S} and O Westergaard",
year = "1990",
month = sep,
day = "20",
doi = "10.1016/S0022-2836(05)80342-0",
language = "English",
volume = "215",
pages = "237--44",
journal = "Journal of Molecular Biology",
issn = "0022-2836",
publisher = "Academic Press",
number = "2",

}

RIS

TY - JOUR

T1 - Characterization of the interaction between topoisomerase II and DNA by transcriptional footprinting

AU - Thomsen, B

AU - Bendixen, C

AU - Lund, K

AU - Andersen, A H

AU - Sørensen, B S

AU - Westergaard, O

PY - 1990/9/20

Y1 - 1990/9/20

N2 - The interaction between calf thymus topoisomerase II and DNA has been characterized using a transcription assay. A highly preferred recognition sequence for topoisomerase II was inserted in either direction downstream from a promoter specific for a bacteriophage RNA polymerase. The presence of topoisomerase II-DNA complexes on the template provoked blockage of transcription, yielding RNA transcripts terminated 5' to the topoisomerase II binding site. A footprint of topoisomerase II, derived from transcription towards the complex from either side, revealed that eukaryotic topoisomerase II binds a region of 28 base-pairs with a highly protected central core of 22 base-pairs. The binding region was located symmetrically around the topoisomerase II-mediated cleavage site. In agreement with this result, optimal topoisomerase II-mediated cleavage was observed with a DNA substrate consisting of a 28-mer oligonucleotide homologous to the protected region. Stepwise removal of base-pairs from the ends of the 28-mer gradually reduced the level of enzyme-mediated cleavage.

AB - The interaction between calf thymus topoisomerase II and DNA has been characterized using a transcription assay. A highly preferred recognition sequence for topoisomerase II was inserted in either direction downstream from a promoter specific for a bacteriophage RNA polymerase. The presence of topoisomerase II-DNA complexes on the template provoked blockage of transcription, yielding RNA transcripts terminated 5' to the topoisomerase II binding site. A footprint of topoisomerase II, derived from transcription towards the complex from either side, revealed that eukaryotic topoisomerase II binds a region of 28 base-pairs with a highly protected central core of 22 base-pairs. The binding region was located symmetrically around the topoisomerase II-mediated cleavage site. In agreement with this result, optimal topoisomerase II-mediated cleavage was observed with a DNA substrate consisting of a 28-mer oligonucleotide homologous to the protected region. Stepwise removal of base-pairs from the ends of the 28-mer gradually reduced the level of enzyme-mediated cleavage.

KW - Acetanilides

KW - Animals

KW - Base Sequence

KW - Binding Sites

KW - Cattle

KW - DNA

KW - DNA Topoisomerases, Type I

KW - DNA-Binding Proteins

KW - In Vitro Techniques

KW - Molecular Sequence Data

KW - Nitroimidazoles

KW - Transcription, Genetic

KW - Journal Article

KW - Research Support, Non-U.S. Gov't

U2 - 10.1016/S0022-2836(05)80342-0

DO - 10.1016/S0022-2836(05)80342-0

M3 - Journal article

C2 - 2170662

VL - 215

SP - 237

EP - 244

JO - Journal of Molecular Biology

JF - Journal of Molecular Biology

SN - 0022-2836

IS - 2

ER -