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Hydroxyl radical "footprinting": high-resolution information about DNA-protein contacts and application to lambda repressor and Cro protein.

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Tullius, T D, Dombroski, B A·1986·Proceedings of the National Academy of Sciences

Abstract

A method has been developed for making "footprints" of proteins bound to DNA. The hydroxyl radical, generated by reduction of hydrogen peroxide by iron(II), is the reagent used to cut the DNA. Hydroxyl radical breaks the backbone of DNA with almost no sequence dependence, so all backbone positions may be monitored for contact with protein. In addition to defining the DNA sequence in contact with the protein, hydroxyl radical footprints embody structural information about the DNA-protein complex. For example, hydroxyl radical footprints of the bacteriophage lambda repressor and Cro protein show directly that these proteins are bound to only one side of the DNA helix. Additional contacts of lambda repressor and Cro protein with DNA, not observed by other chemical footprinting methods, are revealed by hydroxyl radical footprinting.

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Metadata

Authors
Tullius, T. D., & Dombroski, B. A.
Venue
Proceedings of the National Academy of Sciences
Published
1986-08
Volume
83
Issue
15
Pages
5469-5473
ISSN
  • 0027-8424 (ISSN-L)
  • 1091-6490
OpenAlex
W1975329612
Cited by
512
References
0
FWCI
17.16
Type
journal article
Language
en
Open access
green

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CoChat. (2026). Citation check: Hydroxyl radical "footprinting": high-resolution information about DNA-protein contacts and application to lambda repressor and Cro protein. https://app.cochat.ai/papers/10.1073/pnas.83.15.5469
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Tullius, T. D., & Dombroski, B. A. (1986). Hydroxyl radical "footprinting": high-resolution information about DNA-protein contacts and application to lambda repressor and Cro protein. Proceedings of the National Academy of Sciences. https://doi.org/10.1073/pnas.83.15.5469

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Semantic Scholar’s data is described in: Kinney, R., et al. (2023). The Semantic Scholar Open Data Platform. arXiv:2301.10140.