Basic amino acid residues bind to DNA primarily through electrostatic interactions with the phosphate backbone

the verdict

SUPPORTED

the evidence backs this

Recorded sources

3 sources for · 0 against

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Basic amino acid residues play a critical role in DNA binding, relying heavily on positive charges to form electrostatic interactions with the negatively charged phosphate backbone.

The analysis

The retrieved literature consistently supports the principle that positively charged (basic) amino acid residues in proteins facilitate DNA binding predominantly through electrostatic interactions with the negatively charged phosphate backbone. Papers [2], [5], and [8] all explicitly demonstrate or rely on the principle that basic/electropositive residues form ionic bonds with the DNA phosphate backbone, and mutating these residues disrupts binding.

Evidence for · 3

Defining the crucial domain and amino acid residues in bacterial Lon protease for DNA binding and processing of DNA-interacting substrates

Recorded source metadata

Anna Karlowicz, K. Węgrzyn, Marta H. Gross, D. Kaczynska, Malgorzata Ropelewska, Małgorzata Siemiątkowska, J. Bujnicki, I. Konieczny. Defining the crucial domain and amino acid residues in bacterial Lon protease for DNA binding and processing of DNA-interacting substrates. 2017. https://doi.org/10.1074/jbc.M116.766709

Demonstrates that positively charged amino acids are required for DNA binding, as substituting them with negative charges disrupts binding.

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More for · 2

Predicting DNA‐binding amino acid residues from electrostatic stabilization upon mutation to Asp/Glu and evolutionary conservation

Recorded source metadata

Yao Chi Chen, Chih Yuan Wu, Carmay Lim. Predicting DNA‐binding amino acid residues from electrostatic stabilization upon mutation to Asp/Glu and evolutionary conservation. 2007. https://doi.org/10.1002/prot.21366

Notes that the binding of polyanionic DNA relies on clusters of electropositive protein atoms that form stabilizing electrostatic interactions.

Source citation format

Non-specific and specific DNA binding modes of bacterial histone, HU, separately regulate distinct physiological processes through different mechanisms

Recorded source metadata

Subhash C. Verma, Adam Harned, Kedar Narayan, S. Adhya. Non-specific and specific DNA binding modes of bacterial histone, HU, separately regulate distinct physiological processes through different mechanisms. 2023. https://doi.org/10.1111/mmi.15033

Shows that DNA-binding proteins utilize surface-exposed basic residues like lysine to bind the phosphate backbone via ionic bonds.

Source citation format

The paper trail · every fact has a biography

first checked01 Aug 2026

judged → SUPPORTED · 8401 Aug 2026

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