ArticleJournal of molecular biology2009
A DNA-assisted binding assay for weak protein-protein interactions.
Article in Journal of molecular biology, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.
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Who cites it
5 citing papers in PubMed.
- Quantifying Biomolecular Interactions in High-Conductivity Samples With Capillary Electrophoresis.Journal of separation science · 2025Article
- A Careful Insight into DDI-Type Receptor Layers on the Way to Improvement of Click-Biology-Based Immunosensors.Biosensors · 2024Article
- Review
- From adjacent activation in Escherichia coli and DNA cyclization to eukaryotic enhancers: the elements of a puzzle.Frontiers in genetics · 2014Article
- Active role of the interdomain linker of AraC.Journal of bacteriology · 2011Article
Corrections and comments
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Authors and funding
2 authors.
Funding
Abstract
We describe a new method used for quantitating weak interactions between proteins in which the weak interaction is "assisted" by a known DNA-DNA interaction. Oligonucleotides, which are conjugated to proteins of interest, contain short complementary DNA sequences that provide additional binding energy for protein-protein interactions. A stretch of unpaired bases links the protein to the hybridizing DNA sequence to allow formation of both protein-protein and DNA-DNA interactions with minimal structural interference. We validated the DNA-assisted binding method using heterodimerizing coiled-coil proteins. The method was then used to measure the predicted weak interaction between two domains of the Escherichia coli L-arabinose operon regulatory protein AraC. The interaction between domains has the expected magnitude (K(d)=0.37 mM) in the absence of arabinose. Upon addition of arabinose, we detected a weaker and unexpected interaction, which may necessitate modification of the proposed mechanism of AraC. The DNA-assisted binding method may also prove useful in the study of other weak protein-protein interactions.
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