ArticleNucleic acids research2012
Type III restriction endonuclease EcoP15I is a heterotrimeric complex containing one Res subunit with several DNA-binding regions and ATPase activity.
Article in Nucleic acids research, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.
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Who cites it
13 citing papers in PubMed.
- Short-range translocation by a restriction enzyme motor triggers diffusion along DNA.Nature chemical biology · 2024Article
- DciA Helicase Operators Exhibit Diversity across Bacterial Phyla.Journal of bacteriology · 2022Article
- Article
- Structure-Based Deep Mining Reveals First-Time Annotations for 46 Percent of the Dark Annotation Space of the 9,671-Member Superproteome of the Nucleocytoplasmic Large DNA Viruses.Journal of virology · 2020Article
- Genome Sequence of the Urethral Isolate Pseudomonas aeruginosa RN21.Genome announcements · 2015Article
- Structural basis of asymmetric DNA methylation and ATP-triggered long-range diffusion by EcoP15I.Nature communications · 2015Article
- Oligomerization inhibits Legionella pneumophila PlaB phospholipase A activity.The Journal of biological chemistry · 2014Article
- Type III restriction endonucleases are heterotrimeric: comprising one helicase-nuclease subunit and a dimeric methyltransferase that binds only one specific DNA.Nucleic acids research · 2014Article
- Highlights of the DNA cutters: a short history of the restriction enzymes.Nucleic acids research · 2014Article
- Type III restriction-modification enzymes: a historical perspective.Nucleic acids research · 2014Review
- Molecular architecture of the human protein deacetylase Sirt1 and its regulation by AROS and resveratrol.Bioscience reports · 2013Article
- Diverse functions of restriction-modification systems in addition to cellular defense.Microbiology and molecular biology reviews : MMBR · 2013Review
- Structural insights into the assembly and shape of Type III restriction-modification (R-M) EcoP15I complex by small-angle X-ray scattering.Journal of molecular biology · 2012Article
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8 authors.
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Abstract
For efficient DNA cleavage, the Type III restriction endonuclease EcoP15I communicates with two inversely oriented recognition sites in an ATP-dependent process. EcoP15I consists of methylation (Mod) and restriction (Res) subunits forming a multifunctional enzyme complex able to methylate or to cleave DNA. In this study, we determined by different analytical methods that EcoP15I contains a single Res subunit in a Mod(2)Res stoichiometry. The Res subunit comprises a translocase (Tr) domain carrying functional motifs of superfamily 2 helicases and an endonuclease domain with a PD..D/EXK motif. We show that the isolated Tr domain retains ATP-hydrolyzing activity and binds single- and double-stranded DNA in a sequence-independent manner. To localize the regions of DNA binding, we screened peptide arrays representing the entire Res sequence for their ability to interact with DNA. We discovered four DNA-binding regions in the Tr domain and two DNA-binding regions in the endonuclease domain. Modelling of the Tr domain shows that these multiple DNA-binding regions are located on the surface, free to interact with DNA. Interestingly, the positions of the DNA-binding regions are conserved among other Type III restriction endonucleases.
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