ArticleNucleic acids research2016
Novel m4C modification in type I restriction-modification systems.
Article in Nucleic acids research, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.
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.
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.
Who cites it
17 citing papers in PubMed, 29 citations in OpenAlex.
- METTL16 in cancer: Roles and regulatory mechanisms.Genes & diseases · 2026Review
- Bacterial restriction-modification systems: mechanisms of defense against phage infection.Biophysics reports · 2025Article
- The early injected genomic region determines sensitivity to Type I restriction-modification defence against Autographiviridae phages.Nucleic acids research · 2025Article
- TheJournal of bacteriology · 2024Article
- Investigating the mechanism of rough phenotype in a naturally attenuatedFrontiers in medicine · 2024Article
- A sequential one-pot approach for rapid and convenient characterization of putative restriction-modification systems.mSystems · 2023Article
- Acquisition of Type I methyltransferase via horizontal gene transfer increases the drug resistance ofMicrobial genomics · 2023Article
- i4mC-GRU: Identifying DNA NComputational and structural biotechnology journal · 2023Article
- Molecular insights into DNA recognition and methylation by non-canonical type I restriction-modification systems.Nature communications · 2022Article
- A mobile restriction-modification system provides phage defence and resolves an epigenetic conflict with an antagonistic endonuclease.Nucleic acids research · 2022Article
- A novel DNA methylation motif identified in Bacillus pumilus BA06 and possible roles in the regulation of gene expression.Applied microbiology and biotechnology · 2020Article
- Vitamin B and Vitamin C Affect DNA Methylation and Amino Acid Metabolism inFrontiers in microbiology · 2020Article
- Article
- A model for the evolution of prokaryotic DNA restriction-modification systems based upon the structural malleability of Type I restriction-modification enzymes.Nucleic acids research · 2018Article
- N4-cytosine DNA methylation regulates transcription and pathogenesis in Helicobacter pylori.Nucleic acids research · 2018Article
- Structural basis underlying complex assembly and conformational transition of the type I R-M system.Proceedings of the National Academy of Sciences of the United States of America · 2017Article
- DNA target recognition domains in the Type I restriction and modification systems of Staphylococcus aureus.Nucleic acids research · 2017Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
6 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
We identify a new subgroup of Type I Restriction-Modification enzymes that modify cytosine in one DNA strand and adenine in the opposite strand for host protection. Recognition specificity has been determined for ten systems using SMRT sequencing and each recognizes a novel DNA sequence motif. Previously characterized Type I systems use two identical copies of a single methyltransferase (MTase) subunit, with one bound at each half site of the specificity (S) subunit to form the MTase. The new m4C-producing Type I systems we describe have two separate yet highly similar MTase subunits that form a heterodimeric M1M2S MTase. The MTase subunits from these systems group into two families, one of which has NPPF in the highly conserved catalytic motif IV and modifies adenine to m6A, and one having an NPPY catalytic motif IV and modifying cytosine to m4C. The high degree of similarity among their cytosine-recognizing components (MTase and S) suggest they have recently evolved, most likely from the far more common m6A Type I systems. Type I enzymes that modify cytosine exclusively were formed by replacing the adenine target recognition domain (TRD) with a cytosine-recognizing TRD. These are the first examples of m4C modification in Type I RM systems.
Indexed as
Identifiers
What OpenQuestion holds
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.