ArticleNucleic acids research2005
Characterization of the Type III restriction endonuclease PstII from Providencia stuartii.
Article in Nucleic acids research, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 20 papers.
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20 citing papers in PubMed, 27 citations in OpenAlex.
- Eco-evolutionary feedbacks drive the co-occurrence of restriction-modification systems and antimicrobial resistance genes in bacteria.PLoS biology · 2026Article
- Article
- Characterization of the Type III restriction endonuclease PstII from Providencia stuartii.Nucleic acids research · 2019Article
- 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
- Dissociation from DNA of Type III Restriction-Modification enzymes during helicase-dependent motion and following endonuclease activity.Nucleic acids research · 2012Article
- Sequence, structure and functional diversity of PD-(D/E)XK phosphodiesterase superfamily.Nucleic acids research · 2012Article
- 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
- Cloning and characterization of the TneDI restriction: modification system of Thermotoga neapolitana.Extremophiles : life under extreme conditions · 2011Article
- DNA cleavage site selection by Type III restriction enzymes provides evidence for head-on protein collisions following 1D bidirectional motion.Nucleic acids research · 2011Article
- DNA translocation by type III restriction enzymes: a comparison of current models of their operation derived from ensemble and single-molecule measurements.Nucleic acids research · 2011Review
- Translocation, switching and gating: potential roles for ATP in long-range communication on DNA by Type III restriction endonucleases.Biochemical Society transactions · 2011Review
- Type III restriction enzymes cleave DNA by long-range interaction between sites in both head-to-head and tail-to-tail inverted repeat.Proceedings of the National Academy of Sciences of the United States of America · 2010Article
- Maintaining a sense of direction during long-range communication on DNA.Biochemical Society transactions · 2010Review
- The phasevarion: phase variation of type III DNA methyltransferases controls coordinated switching in multiple genes.Nature reviews. Microbiology · 2010Review
- DNA cleavage and methylation specificity of the single polypeptide restriction-modification enzyme LlaGI.Nucleic acids research · 2009Article
- S-adenosyl homocysteine and DNA ends stimulate promiscuous nuclease activities in the Type III restriction endonuclease EcoPI.Nucleic acids research · 2009Article
- Type III restriction enzymes communicate in 1D without looping between their target sites.Proceedings of the National Academy of Sciences of the United States of America · 2009Article
- DNA looping and translocation provide an optimal cleavage mechanism for the type III restriction enzymes.The EMBO journal · 2007Article
- Selection of restriction endonucleases using artificial cells.Nucleic acids research · 2007Article
- Subunit assembly modulates the activities of the Type III restriction-modification enzyme PstII in vitro.Nucleic acids research · 2005Article
Corrections and comments
- Erratum issued
Authors and funding
4 authors at 2 institutions in 2 countries.
Funding
Abstract
A new Type III restriction endonuclease designated PstII has been purified from Providencia stuartii. PstII recognizes the hexanucleotide sequence 5'-CTGATG(N)(25-26/27-28)-3'. Endonuclease activity requires a substrate with two copies of the recognition site in head-to-head repeat and is dependent on a low level of ATP hydrolysis ( approximately 40 ATP/site/min). Cleavage occurs at just one of the two sites and results in a staggered cut 25-26 nt downstream of the top strand sequence to generate a two base 5'-protruding end. Methylation of the site occurs on one strand only at the first adenine of 5'-CATCAG-3'. Therefore, PstII has characteristic Type III restriction enzyme activity as exemplified by EcoPI or EcoP15I. Moreover, sequence asymmetry of the PstII recognition site in the T7 genome acts as an historical imprint of Type III restriction activity in vivo. In contrast to other Type I and III enzymes, PstII has a more relaxed nucleotide specificity and can cut DNA with GTP and CTP (but not UTP). We also demonstrate that PstII and EcoP15I cannot interact and cleave a DNA substrate suggesting that Type III enzymes must make specific protein-protein contacts to activate endonuclease activity.
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