ArticleNature structural & molecular biology2009
Structure of the motor subunit of type I restriction-modification complex EcoR124I.
Article in Nature structural & molecular biology, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 29 papers.
What it found
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Who cites it
29 citing papers in PubMed.
- Molecular insights into DNA recognition and methylation by non-canonical type I restriction-modification systems.Nature communications · 2022Article
- Structural insights into assembly, operation and inhibition of a type I restriction-modification system.Nature microbiology · 2020Article
- 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
- 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
- A residue of motif III positions the helicase domains of motor subunit HsdR in restriction-modification enzyme EcoR124I.Journal of molecular modeling · 2018Article
- The H-subunit of the restriction endonuclease CglI contains a prototype DEAD-Z1 helicase-like motor.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
- 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
- Genome-wide survey of codons under diversifying selection in a highly recombining bacterial species, Helicobacter pylori.DNA research : an international journal for rapid publication of reports on genes and genomes · 2016Article
- Functional coupling of duplex translocation to DNA cleavage in a type I restriction enzyme.PloS one · 2015Article
- Crystal structure of the R-protein of the multisubunit ATP-dependent restriction endonuclease NgoAVII.Nucleic acids research · 2014Article
- Interdomain communication in the endonuclease/motor subunit of type I restriction-modification enzyme EcoR124I.Journal of molecular modeling · 2014Article
- Cloning, crystallization and preliminary X-ray diffraction analysis of an intact DNA methyltransferase of a type I restriction-modification enzyme from Vibrio vulnificus.Acta crystallographica. Section F, Structural biology communications · 2014Article
- Type I restriction enzymes and their relatives.Nucleic acids research · 2014Review
- Duplex RNA activated ATPases (DRAs): platforms for RNA sensing, signaling and processing.RNA biology · 2013Review
- Sequence, structure and functional diversity of PD-(D/E)XK phosphodiesterase superfamily.Nucleic acids research · 2012Article
- Superfamily 2 helicases.Frontiers in bioscience (Landmark edition) · 2012Review
- Type III restriction endonuclease EcoP15I is a heterotrimeric complex containing one Res subunit with several DNA-binding regions and ATPase activity.Nucleic acids research · 2012Article
- Adenine recognition is a key checkpoint in the energy release mechanism of phage T4 DNA packaging motor.Journal of molecular biology · 2012Article
Corrections and comments
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Authors and funding
7 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Type I restriction-modification enzymes act as conventional adenine methylases on hemimethylated DNAs, but unmethylated recognition targets induce them to translocate thousands of base pairs before cleaving distant sites nonspecifically. The first crystal structure of a type I motor subunit responsible for translocation and cleavage suggests how the pentameric translocating complex is assembled and provides a structural framework for translocation of duplex DNA by RecA-like ATPase motors.
Indexed as
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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.