September 5, 2025Open Access

A basic leucine zipper uses a dimer pathway to locate its targets in DNA mixtures

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In vitro measurements revealed CREB dimer enhances DNA binding efficiency in eukaryotic systems, suggesting implications for transcriptional control.

Dimeric CREB shows significantly improved DNA binding efficiency compared to its monomeric form, enhancing target search.
Kinetic data revealed that the preference for dimeric mechanisms occurs with a relative flux of only 1 in 10,000 for monomeric pathways.
Equilibrium experiments suggest this dimerization preference is a common feature among basic leucine zipper proteins.
Findings may inform the design of artificial transcription factors and inhibitors through improved understanding of DNA binding mechanics.

Kuravsky et al. (2025) studied this question.

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September 5, 2025Open Access

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Authors

In vitro measurements revealed CREB dimer enhances DNA binding efficiency in eukaryotic systems, suggesting implications for transcriptional control.

Dimeric CREB shows significantly improved DNA binding efficiency compared to its monomeric form, enhancing target search.
Kinetic data revealed that the preference for dimeric mechanisms occurs with a relative flux of only 1 in 10,000 for monomeric pathways.
Equilibrium experiments suggest this dimerization preference is a common feature among basic leucine zipper proteins.
Findings may inform the design of artificial transcription factors and inhibitors through improved understanding of DNA binding mechanics.

Kuravsky et al. (2025) studied this question.

View Full Paper

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