ArticlePloS one2010
Cofactor requirement of HpyAV restriction endonuclease.
Article in PloS one, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.
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Who cites it
19 citing papers in PubMed.
- Argonaute-HNH filaments triggered by invader DNA confer bacterial immunity.Nature communications · 2025Article
- Identification and characterization of a new HNH restriction endonuclease with unusual properties.Applied microbiology and biotechnology · 2023Article
- Promiscuous DNA cleavage by HpyAII endonuclease is modulated by the HNH catalytic residues.Bioscience reports · 2020Article
- Type II Restriction-Modification System fromPathogens (Basel, Switzerland) · 2020Article
- Protein Domain Guided Screen for Sequence Specific and Phosphorothioate-Dependent Restriction Endonucleases.Frontiers in microbiology · 2020Article
- Expression and purification of a single-chain Type IV restriction enzyme Eco94GmrSD and determination of its substrate preference.Scientific reports · 2015Article
- Metalloregulation of Helicobacter pylori physiology and pathogenesis.Frontiers in microbiology · 2015Review
- Frequency of TERT promoter mutations in primary tumors of the liver.Virchows Archiv : an international journal of pathology · 2014Article
- Type II restriction endonucleases--a historical perspective and more.Nucleic acids research · 2014Review
- Structure of 5-hydroxymethylcytosine-specific restriction enzyme, AbaSI, in complex with DNA.Nucleic acids research · 2014Article
- Engineering nicking enzymes that preferentially nick 5-methylcytosine-modified DNA.Nucleic acids research · 2014Article
- Elimination of inter-domain interactions increases the cleavage fidelity of the restriction endonuclease DraIII.Protein & cell · 2014Article
- Highlights of the DNA cutters: a short history of the restriction enzymes.Nucleic acids research · 2014Article
- The other face of restriction: modification-dependent enzymes.Nucleic acids research · 2014Review
- Increasing cleavage specificity and activity of restriction endonuclease KpnI.Nucleic acids research · 2013Article
- Natural zinc ribbon HNH endonucleases and engineered zinc finger nicking endonuclease.Nucleic acids research · 2013Article
- A type IV modification-dependent restriction enzyme SauUSI from Staphylococcus aureus subsp. aureus USA300.Nucleic acids research · 2011Article
- Functional analysis of an acid adaptive DNA adenine methyltransferase from Helicobacter pylori 26695.PloS one · 2011Article
- Cleavage of phosphorothioated DNA and methylated DNA by the type IV restriction endonuclease ScoMcrA.PLoS genetics · 2010Article
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Authors and funding
5 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
backgroundHelicobacter pylori is the etiologic agent of common gastritis and a risk factor for gastric cancer. It is also one of the richest sources of Type II restriction-modification (R-M) systems in microorganisms. PRINCIPAL
findingsWe have cloned, expressed and purified a new restriction endonuclease HpyAV from H. pylori strain 26695. We determined the HpyAV DNA recognition sequence and cleavage site as CCTTC 6/5. In addition, we found that HpyAV has a unique metal ion requirement: its cleavage activity is higher with transition metal ions than in Mg(++). The special metal ion requirement of HpyAV can be attributed to the presence of a HNH catalytic site similar to ColE9 nuclease instead of the canonical PD-X-D/EXK catalytic site found in many other REases. Site-directed mutagenesis was carried out to verify the catalytic residues of HpyAV. Mutation of the conserved metal-binding Asn311 and His320 to alanine eliminated cleavage activity. HpyAV variant H295A displayed approximately 1% of wt activity. CONCLUSIONS/SIGNIFICANCE: Some HNH-type endonucleases have unique metal ion cofactor requirement for optimal activities. Homology modeling and site-directed mutagenesis confirmed that HpyAV is a member of the HNH nuclease family. The identification of catalytic residues in HpyAV paved the way for further engineering of the metal binding site. A survey of sequenced microbial genomes uncovered 10 putative R-M systems that show high sequence similarity to the HpyAV system, suggesting lateral transfer of a prototypic HpyAV-like R-M system among these microorganisms.
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