ReviewNucleic acids research2001
Nucleoside triphosphate-dependent restriction enzymes.
Review in Nucleic acids research, 2001. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 78 papers.
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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.
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Who cites it
78 citing papers in PubMed, 160 citations in OpenAlex.
- Single Staphylococcus aureus SauUSI restriction enzyme motors fragment methylated DNA.Nature chemical biology · 2026Article
- ssDNA phage FLiP resides in dsDNA form in resistant Flavobacterium host.Biology direct · 2025Article
- Adapting recombinant bacterial alkaline phosphatase for nucleotide exchange of small GTPases.Protein expression and purification · 2024Article
- Review
- Bacterial DNA methyltransferase: A key to the epigenetic world with lessons learned from proteobacteria.Frontiers in microbiology · 2023Review
- Advanced biotechnology using methyltransferase and its applications in bacteria: a mini review.Biotechnology letters · 2022Review
- Mechanism of DNA cleavage by the endonuclease SauUSI: a major barrier to horizontal gene transfer and antibiotic resistance in Staphylococcus aureus.Nucleic acids research · 2021Article
- The N-terminal domain of Staphylothermus marinus McrB shares structural homology with PUA-like RNA binding proteins.Journal of structural biology · 2020Article
- The structure of theThe Journal of biological chemistry · 2020Article
- Functional screening of a soil metagenome for DNA endonucleases by acquired resistance to bacteriophage infection.Molecular biology reports · 2020Article
- Metabolic engineering of Bacillus amyloliquefaciens LL3 for enhanced poly-γ-glutamic acid synthesis.Microbial biotechnology · 2019Article
- Article
- Crystal structure of a novel domain of the motor subunit of the Type I restriction enzyme EcoR124 involved in complex assembly and DNA binding.The Journal of biological chemistry · 2018Article
- The helical domain of the EcoR124I motor subunit participates in ATPase activity and dsDNA translocation.PeerJ · 2017Article
- pHluorin-assisted expression, purification, crystallization and X-ray diffraction data analysis of the C-terminal domain of the HsdR subunit of the Escherichia coli type I restriction-modification system EcoR124I.Acta crystallographica. Section F, Structural biology communications · 2016Article
- SMRT sequencing of the Campylobacter coli BfR-CA-9557 genome sequence reveals unique methylation motifs.BMC genomics · 2015Article
- Translocation-coupled DNA cleavage by the Type ISP restriction-modification enzymes.Nature chemical biology · 2015Article
- Article
- Type III Methyltransferase M.NgoAX from Neisseria gonorrhoeae FA1090 Regulates Biofilm Formation and Interactions with Human Cells.Frontiers in microbiology · 2015Article
- TstI, a Type II restriction-modification protein with DNA recognition, cleavage and methylation functions in a single polypeptide.Nucleic acids research · 2014Article
18 more citing papers are in PubMed but not listed here.
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
3 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The known nucleoside triphosphate-dependent restriction enzymes are hetero-oligomeric proteins that behave as molecular machines in response to their target sequences. They translocate DNA in a process dependent on the hydrolysis of a nucleoside triphosphate. For the ATP-dependent type I and type III restriction and modification systems, the collision of translocating complexes triggers hydrolysis of phosphodiester bonds in unmodified DNA to generate double-strand breaks. Type I endonucleases break the DNA at unspecified sequences remote from the target sequence, type III endonucleases at a fixed position close to the target sequence. Type I and type III restriction and modification (R-M) systems are notable for effective post-translational control of their endonuclease activity. For some type I enzymes, this control is mediated by proteolytic degradation of that subunit of the complex which is essential for DNA translocation and breakage. This control, lacking in the well-studied type II R-M systems, provides extraordinarily effective protection of resident DNA should it acquire unmodified target sequences. The only well-documented GTP-dependent restriction enzyme, McrBC, requires methylated target sequences for the initiation of phosphodiester bond cleavage.
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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.