Evidence map›Paper›PMID 25845600›Full record

ArticleNucleic acids research2015

Structures of Escherichia coli DNA adenine methyltransferase (Dam) in complex with a non-GATC sequence: potential implications for methylation-independent transcriptional repression.

John R Horton, Xing Zhang, Robert M Blumenthal, Xiaodong Cheng

Open access · goldAbstract read
In one paragraph

Article in Nucleic acids research, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.

0numbers the graph read from it
0cells of the map it votes in
14citing papers in PubMed
0.3field-weighted citation impact, top 38% 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

14 citing papers in PubMed, 17 citations in OpenAlex.

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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

4 authors at 2 institutions in 1 country.

John R HortonDepartment of Biochemistry, Emory University School of Medicine, Atlanta, GA 30322, USA.
Xing ZhangDepartment of Biochemistry, Emory University School of Medicine, Atlanta, GA 30322, USA.
Robert M BlumenthalDepartment of Medical Microbiology and Immunology and Program in Bioinformatics, The University of Toledo College of Medicine and Life Sciences, Toledo, OH 43614, USA.
Xiaodong ChengDepartment of Biochemistry, Emory University School of Medicine, Atlanta, GA 30322, USA xcheng@emory.edu.
Emory University · USUniversity of Toledo · US

Funding

THREE-DIMENSIONAL STRUCTURE OF HHAI METHYLASER01GM049245 · NIGMS · UNIVERSITY OF TX MD ANDERSON CAN CTR · PI CHENG, XIAODONG · 1993 to 2017
$6.6M
NIGMS NIH HHS GM049245-21NIGMS NIH HHS R01 GM049245
6 · The paper itself

Abstract

DNA adenine methyltransferase (Dam) is widespread and conserved among the γ-proteobacteria. Methylation of the Ade in GATC sequences regulates diverse bacterial cell functions, including gene expression, mismatch repair and chromosome replication. Dam also controls virulence in many pathogenic Gram-negative bacteria. An unexplained and perplexing observation about Escherichia coli Dam (EcoDam) is that there is no obvious relationship between the genes that are transcriptionally responsive to Dam and the promoter-proximal presence of GATC sequences. Here, we demonstrate that EcoDam interacts with a 5-base pair non-cognate sequence distinct from GATC. The crystal structure of a non-cognate complex allowed us to identify a DNA binding element, GTYTA/TARAC (where Y = C/T and R = A/G). This element immediately flanks GATC sites in some Dam-regulated promoters, including the Pap operon which specifies pyelonephritis-associated pili. In addition, Dam interacts with near-cognate GATC sequences (i.e. 3/4-site ATC and GAT). Taken together, these results imply that Dam, in addition to being responsible for GATC methylation, could also function as a methylation-independent transcriptional repressor.

Indexed as

Base SequenceBinding SitesDNA, BacterialEscherichia coliEscherichia coli ProteinsGene Expression Regulation, BacterialModels, MolecularNucleic Acid ConformationPromoter Regions, GeneticRepressor ProteinsSite-Specific DNA-Methyltransferase (Adenine-Specific)dam protein, E coliDNA, BacterialEscherichia coli ProteinsRepressor ProteinsSite-Specific DNA-Methyltransferase (Adenine-Specific)

Identifiers

PMID25845600
PMCPMC4417163
OpenAlexW2160150996

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC
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.