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Structure-specific binding of the proto-oncogene protein DEK to DNA

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2003

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Nucleic Acids Research. 2003, 31(23), pp. 7003-7010. ISSN 0305-1048. eISSN 1362-4962. Available under: doi: 10.1093/nar/gkg864

Zusammenfassung

The ubiquitous proto-oncogene protein DEK has been found to be associated with chromatin during the entire cell cycle. It changes the topology of DNA in chromatin and protein-free DNA through the introduction of positive supercoils. The sequence and structure specificities of DEK-DNA interactions are not completely understood. The binding of DEK to DNA is not sequence specific, but we describe here that DEK has a clear preference for supercoiled and four-way junction DNA. In the presence of topoisomerase II, DEK stimulates intermolecular catenation of circular DNA molecules. DEK also increases the probability of intermolecular ligation of linear DNA molecules by DNA ligase. These binding properties qualify DEK as an architectural protein.

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570 Biowissenschaften, Biologie

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ISO 690WALDMANN, Tanja, Martina BAACK, Nicole RICHTER, Claudia GRUSS, 2003. Structure-specific binding of the proto-oncogene protein DEK to DNA. In: Nucleic Acids Research. 2003, 31(23), pp. 7003-7010. ISSN 0305-1048. eISSN 1362-4962. Available under: doi: 10.1093/nar/gkg864
BibTex
@article{Waldmann2003-12-01Struc-39001,
  year={2003},
  doi={10.1093/nar/gkg864},
  title={Structure-specific binding of the proto-oncogene protein DEK to DNA},
  number={23},
  volume={31},
  issn={0305-1048},
  journal={Nucleic Acids Research},
  pages={7003--7010},
  author={Waldmann, Tanja and Baack, Martina and Richter, Nicole and Gruss, Claudia}
}
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    <dcterms:abstract xml:lang="eng">The ubiquitous proto-oncogene protein DEK has been found to be associated with chromatin during the entire cell cycle. It changes the topology of DNA in chromatin and protein-free DNA through the introduction of positive supercoils. The sequence and structure specificities of DEK-DNA interactions are not completely understood. The binding of DEK to DNA is not sequence specific, but we describe here that DEK has a clear preference for supercoiled and four-way junction DNA. In the presence of topoisomerase II, DEK stimulates intermolecular catenation of circular DNA molecules. DEK also increases the probability of intermolecular ligation of linear DNA molecules by DNA ligase. These binding properties qualify DEK as an architectural protein.</dcterms:abstract>
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