ArticleNucleic acids research2009
The fragment structure of a putative HsdR subunit of a type I restriction enzyme from Vibrio vulnificus YJ016: implications for DNA restriction and translocation activity.
Article in Nucleic acids research, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.
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17 citing papers in PubMed, 27 citations in OpenAlex.
- Article
- Molecular insights into DNA recognition and methylation by non-canonical type I restriction-modification systems.Nature communications · 2022Article
- 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
- Structural insights into assembly, operation and inhibition of a type I restriction-modification system.Nature microbiology · 2020Article
- Combinations ofeLife · 2019Article
- 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
- 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
- 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
- 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
- Structural and functional analysis of the symmetrical Type I restriction endonuclease R.EcoR124IPloS one · 2012Article
- Structure and operation of the DNA-translocating type I DNA restriction enzymes.Genes & development · 2012Article
- Characterization and crystal structure of the type IIG restriction endonuclease RM.BpuSI.Nucleic acids research · 2011Article
- Structural and functional analysis of the engineered type I DNA methyltransferase EcoR124IJournal of molecular biology · 2010Article
- Maintaining a sense of direction during long-range communication on DNA.Biochemical Society transactions · 2010Review
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6 authors at 1 institution in 1 country.
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No grant is acknowledged in the PubMed record.
Abstract
Among four types of bacterial restriction enzymes that cleave a foreign DNA depending on its methylation status, type I enzymes composed of three subunits are interesting because of their unique DNA cleavage and translocation mechanisms performed by the restriction subunit (HsdR). The elucidated N-terminal fragment structure of a putative HsdR subunit from Vibrio vulnificus YJ016 reveals three globular domains. The nucleolytic core within an N-terminal nuclease domain (NTD) is composed of one basic and three acidic residues, which include a metal-binding site. An ATP hydrolase (ATPase) site at the interface of two RecA-like domains (RDs) is located close to the probable DNA-binding site for translocation, which is far from the NTD nucleolytic core. Comparison of relative domain arrangements with other functionally related ATP and/or DNA complex structures suggests a possible translocation and restriction mechanism of the HsdR subunit. Furthermore, careful analysis of its sequence and structure implies that a linker helix connecting two RDs and an extended region within the nuclease domain may play a central role in switching the DNA translocation into the restriction activity.
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