Evidence map›Paper›PMID 34103525›Full record

ArticleNature communications2021

Clostridioides difficile specific DNA adenine methyltransferase CamA squeezes and flips adenine out of DNA helix.

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

Open access · goldAbstract read
In one paragraph

Article in Nature communications, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.

0numbers the graph read from it
0cells of the map it votes in
23citing papers in PubMed
1.6field-weighted citation impact, top 14% 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

23 citing papers in PubMed, 29 citations in OpenAlex.

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  15. Systematic Design of Adenosine Analogs as Inhibitors of aJournal of medicinal chemistry · 2023
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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

5 authors at 2 institutions in 1 country.

Jujun Zhou *Department of Epigenetics and Molecular Carcinogenesis, University of Texas MD Anderson Cancer Center, Houston, TX, USA.ORCID 0000-0003-4104-7158
John R Horton *Department of Epigenetics and Molecular Carcinogenesis, University of Texas MD Anderson Cancer Center, Houston, TX, USA.ORCID 0000-0001-9749-8068
Robert M BlumenthalDepartment of Medical Microbiology and Immunology, and Program in Bioinformatics, The University of Toledo College of Medicine and Life Sciences, Toledo, OH, USA.
Xing ZhangDepartment of Epigenetics and Molecular Carcinogenesis, University of Texas MD Anderson Cancer Center, Houston, TX, USA. XZhang21@mdanderson.org.
Xiaodong ChengDepartment of Epigenetics and Molecular Carcinogenesis, University of Texas MD Anderson Cancer Center, Houston, TX, USA. XCheng5@mdanderson.org.ORCID 0000-0002-6967-6362
The University of Texas MD Anderson Cancer Center · USUniversity of Toledo · US

Funding

Epigenetic regulations of DNA and histone methylation and deMethylation: Structures and MechanismsR35GM134744 · NIGMS · UNIVERSITY OF TX MD ANDERSON CAN CTR · PI Xiaodong Cheng · 2020 to 2026
$4.5M
NIGMS NIH HHS R35 GM134744
6 · The paper itself

Abstract

Clostridioides difficile infections are an urgent medical problem. The newly discovered C. difficile adenine methyltransferase A (CamA) is specified by all C. difficile genomes sequenced to date (>300), but is rare among other bacteria. CamA is an orphan methyltransferase, unassociated with a restriction endonuclease. CamA-mediated methylation at CAAAAA is required for normal sporulation, biofilm formation, and intestinal colonization by C. difficile. We characterized CamA kinetic parameters, and determined its structure bound to DNA containing the recognition sequence. CamA contains an N-terminal domain for catalyzing methyl transfer, and a C-terminal DNA recognition domain. Major and minor groove DNA contacts in the recognition site involve base-specific hydrogen bonds, van der Waals contacts and the Watson-Crick pairing of a rearranged A:T base pair. These provide sufficient sequence discrimination to ensure high specificity. Finally, the surprisingly weak binding of the methyl donor S-adenosyl-L-methionine (SAM) might provide avenues for inhibiting CamA activity using SAM analogs.

Indexed as

Nucleic Acid ConformationAdenineBase PairingBase SequenceClostridioidesCoenzymesDNA, BacterialModels, MolecularNucleotide MotifsS-AdenosylhomocysteineSite-Specific DNA-Methyltransferase (Adenine-Specific)Species SpecificitySubstrate SpecificityAdenineCoenzymesDNA, BacterialS-AdenosylhomocysteineSite-Specific DNA-Methyltransferase (Adenine-Specific)

Identifiers

PMID34103525
PMCPMC8187626
OpenAlexW3172614539

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.