ArticleThe FEBS journal2013
pH modulates the binding of early growth response protein 1 transcription factor to DNA.
Article in The FEBS journal, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
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Who cites it
11 citing papers in PubMed, 18 citations in OpenAlex.
- Probing the role of the protonation state of a minor groove-linker histidine in Exd-Hox-DNA binding.Biophysical journal · 2024Article
- How protons pave the way to aggressive cancers.Nature reviews. Cancer · 2023Review
- Nucleic acid-induced dimerization of HIV-1 Gag protein.The Journal of biological chemistry · 2019Article
- DNA-protein interaction: identification, prediction and data analysis.Molecular biology reports · 2019Review
- Article
- Ehrlichia chaffeensis TRP120 nucleomodulin binds DNA with disordered tandem repeat domain.PloS one · 2018Article
- Nuclear proton dynamics and interactions with calcium signaling.Journal of molecular and cellular cardiology · 2016Article
- Effect of osmolytes on the binding of EGR1 transcription factor to DNA.Biopolymers · 2015Article
- Role of promoter DNA sequence variations on the binding of EGR1 transcription factor.Archives of biochemistry and biophysics · 2014Article
- Enthalpic factors override the polyelectrolyte effect in the binding of EGR1 transcription factor to DNA.Journal of molecular recognition : JMR · 2014Article
- RNA binding of T-cell intracellular antigen-1 (TIA-1) C-terminal RNA recognition motif is modified by pH conditions.The Journal of biological chemistry · 2013Article
Corrections and comments
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Authors and funding
7 authors at 1 institution in 1 country.
Funding
Abstract
The transcription factor early growth response protein (EGR)1 orchestrates a plethora of signaling cascades involved in cellular homeostasis, and its downregulation has been implicated in the development of prostate cancer. Herein, using a battery of biophysical tools, we show that the binding of EGR1 to DNA is tightly regulated by solution pH. Importantly, the binding affinity undergoes an enhancement of more than an order of magnitude with an increase in pH from 5 to 8, implying that the deprotonation of an ionizable residue accounts for such behavior. This ionizable residue is identified as His382 by virtue of the fact that its replacement by nonionizable residues abolishes the pH dependence of the binding of EGR1 to DNA. Notably, His382 inserts into the major groove of DNA, and stabilizes the EGR1-DNA interaction via both hydrogen bonding and van der Waals contacts. Remarkably, His382 is mainly conserved across other members of the EGR family, implying that histidine protonation-deprotonation may serve as a molecular switch for modulating the protein-DNA interactions that are central to this family of transcription factors. Collectively, our findings reveal an unexpected but a key step in the molecular recognition of the EGR family of transcription factors, and suggest that they may act as sensors of pH within the intracellular environment.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.