Evidence map›Paper›PMID 38042148›Full record

ArticleStructure (London, England : 1993)2024

Dissection of integrated readout reveals the structural thermodynamics of DNA selection by transcription factors.

Tyler N Vernon, J Ross Terrell, Amanda V Albrecht, Markus W Germann, W David Wilson, Gregory M K Poon

Open access · greenAbstract read
In one paragraph

Article in Structure (London, England : 1993), 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.

0numbers the graph read from it
0cells of the map it votes in
3citing papers in PubMed
0.6field-weighted citation impact, top 29% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

3 citing papers in PubMed, 4 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

6 authors at 1 institution in 1 country.

Tyler N VernonDepartment of Chemistry, Georgia State University, Atlanta, GA 30302, USA.
J Ross TerrellDepartment of Chemistry, Georgia State University, Atlanta, GA 30302, USA.
Amanda V AlbrechtDepartment of Chemistry, Georgia State University, Atlanta, GA 30302, USA.
Markus W GermannDepartment of Chemistry, Georgia State University, Atlanta, GA 30302, USA; Department of Biology, Georgia State University, Atlanta, GA 30302, USA. Electronic address: mwg@gsu.edu.
W David WilsonDepartment of Chemistry, Georgia State University, Atlanta, GA 30302, USA; Center for Diagnostics and Therapeutics, Georgia State University, Atlanta, GA 30302, USA. Electronic address: wdw@gsu.edu.
Gregory M K PoonDepartment of Chemistry, Georgia State University, Atlanta, GA 30302, USA; Center for Diagnostics and Therapeutics, Georgia State University, Atlanta, GA 30302, USA. Electronic address: gpoon@gsu.edu.
Georgia State University · US

Funding

Direct chemical control of the hematopoietic master transcription factor PU.1R01HL155178 · NHLBI · GEORGIA STATE UNIVERSITY · PI POON, GREGORY MAN KAI · 2021 to 2023
$1.2M
NHLBI NIH HHS R01 HL155178
6 · The paper itself

Abstract

Nucleobases such as inosine have been extensively utilized to map direct contacts by proteins in the DNA groove. Their deployment as targeted probes of dynamics and hydration, which are dominant thermodynamic drivers of affinity and specificity, has been limited by a paucity of suitable experimental models. We report a joint crystallographic, thermodynamic, and computational study of the bidentate complex of the arginine side chain with a Watson-Crick guanine (Arg×GC), a highly specific configuration adopted by major transcription factors throughout the eukaryotic branches in the Tree of Life. Using the ETS-family factor PU.1 as a high-resolution structural framework, inosine substitution for guanine resulted in a sharp dissection of conformational dynamics and hydration and elucidated their role in the DNA specificity of PU.1. Our work suggests an under-exploited utility of modified nucleobases in untangling the structural thermodynamics of interactions, such as the Arg×GC motif, where direct and indirect readout are tightly integrated.

Indexed as

Proto-Oncogene ProteinsTranscription FactorsBinding SitesDNAGuanineInosineNucleic Acid ConformationProtein BindingThermodynamicsDNAGuanineInosineProto-Oncogene ProteinsTranscription Factorsconformational dynamicsDNA readoutmodified nucleobasesmolecular hydrationprotein-DNA recognitionPU.1specificitystructural thermodynamics

Identifiers

PMID38042148
PMCPMC12924625
OpenAlexW4389247261

What OpenQuestion holds

Textmetadata
LicenceTDM
Read underepoch 390

Registered trials

None linked

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.