Evidence map›Paper›PMID 17605809›Full record

ArticleBMC molecular biology2007

Vertebrate DM domain proteins bind similar DNA sequences and can heterodimerize on DNA.

Mark W Murphy, David Zarkower, Vivian J Bardwell

Open access · hybridAbstract read
In one paragraph

Article in BMC molecular biology, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 51 papers.

0numbers the graph read from it
0cells of the map it votes in
51citing papers in PubMed
3.4field-weighted citation impact, top 7% 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

51 citing papers in PubMed, 97 citations in OpenAlex.

  1. Review
  2. Article
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  6. Novel Insights into Emx2 and Dmrta2 Cooperation during Cortex Development and Evidence for Dmrta2 Function in the Choroid Plexus.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2025
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  12. Analyses of theFrontiers in physiology · 2023
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  13. Article
  14. Review
  15. Review
  16. Identification of Sex-Related Genes from the Three-Spot Swimming CrabAnimals : an open access journal from MDPI · 2021
    Article
  17. Article
  18. Article
  19. Article
  20. Multiple Functions of theFrontiers in neuroscience · 2021
    Review
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

3 authors at 1 institution in 1 country.

Mark W MurphyDept. of Genetics, Cell Biology, and Development, University of Minnesota, Minneapolis, MN 55455, USA. murph035@umn.edu <murph035@umn.edu>
David Zarkower
Vivian J Bardwell
University of Minnesota · US

Funding

DMRT1 IN MAMMALIAN SEXUAL DEVELOPMENTR01GM059152 · NIGMS · UNIVERSITY OF MINNESOTA TWIN CITIES · PI BARDWELL, VIVIAN J, ZARKOWER, DAVID A. · 1999 to 2019
$8.8M
NIGMS NIH HHS GM59152NIGMS NIH HHS R01 GM059152
6 · The paper itself

Abstract

backgroundThe DM domain is a zinc finger-like DNA binding motif first identified in the sexual regulatory proteins Doublesex (DSX) and MAB-3, and is widely conserved among metazoans. DM domain proteins regulate sexual differentiation in at least three phyla and also control other aspects of development, including vertebrate segmentation. Most DM domain proteins share little similarity outside the DM domain. DSX and MAB-3 bind partially overlapping DNA sequences, and DSX has been shown to interact with DNA via the minor groove without inducing DNA bending. DSX and MAB-3 exhibit unusually high DNA sequence specificity relative to other minor groove binding proteins. No detailed analysis of DNA binding by the seven vertebrate DM domain proteins, DMRT1-DMRT7 has been reported, and thus it is unknown whether they recognize similar or diverse DNA sequences.

resultsWe used a random oligonucleotide in vitro selection method to determine DNA binding sites for six of the seven proteins. These proteins selected sites resembling that of DSX despite differences in the sequence of the DM domain recognition helix, but they varied in binding efficiency and in preferences for particular nucleotides, and some behaved anomalously in gel mobility shift assays. DMRT1 protein from mouse testis extracts binds the sequence we determined, and the DMRT proteins can bind their in vitro-defined sites in transfected cells. We also find that some DMRT proteins can bind DNA as heterodimers.

conclusionOur results suggest that target gene specificity of the DMRT proteins does not derive exclusively from major differences in DNA binding specificity. Instead target specificity may come from more subtle differences in DNA binding preference between different homodimers, together with differences in binding specificity between homodimers versus heterodimers.

Indexed as

AnimalsBinding SitesDimerizationDNAMaleMiceOligonucleotidesProtein Structure, TertiaryTestisTranscription FactorsDMRT1 proteinDmrt3 protein, mouseDNAOligonucleotidesTranscription Factors

Identifiers

PMID17605809
PMCPMC1931443
OpenAlexW1988748038

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.