ArticleNucleic acids research2011
Recycling of protein subunits during DNA translocation and cleavage by Type I restriction-modification enzymes.
Article in Nucleic acids research, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
What it found
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Who cites it
9 citing papers in PubMed, 11 citations in OpenAlex.
- Biology of host-dependent restriction-modification in prokaryotes.EcoSal Plus · 2025Review
- CgII cleaves DNA using a mechanism distinct from other ATP-dependent restriction endonucleases.Nucleic acids research · 2017Article
- The helical domain of the EcoR124I motor subunit participates in ATPase activity and dsDNA translocation.PeerJ · 2017Article
- ClpXP protease targets long-lived DNA translocation states of a helicase-like motor to cause restriction alleviation.Nucleic acids research · 2014Article
- Article
- Transposon mutagenesis identified chromosomal and plasmid genes essential for adaptation of the marine bacterium Dinoroseobacter shibae to anaerobic conditions.Journal of bacteriology · 2013Article
- Dissociation from DNA of Type III Restriction-Modification enzymes during helicase-dependent motion and following endonuclease activity.Nucleic acids research · 2012Article
- Structure and operation of the DNA-translocating type I DNA restriction enzymes.Genes & development · 2012Article
- Genetic manipulation of Staphylococci-breaking through the barrier.Frontiers in cellular and infection microbiology · 2012Review
Corrections and comments
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
The Type I restriction-modification enzymes comprise three protein subunits; HsdS and HsdM that form a methyltransferase (MTase) and HsdR that associates with the MTase and catalyses Adenosine-5'-triphosphate (ATP)-dependent DNA translocation and cleavage. Here, we examine whether the MTase and HsdR components can 'turnover' in vitro, i.e. whether they can catalyse translocation and cleavage events on one DNA molecule, dissociate and then re-bind a second DNA molecule. Translocation termination by both EcoKI and EcoR124I leads to HsdR dissociation from linear DNA but not from circular DNA. Following DNA cleavage, the HsdR subunits appear unable to dissociate even though the DNA is linear, suggesting a tight interaction with the cleaved product. The MTases of EcoKI and EcoAI can dissociate from DNA following either translocation or cleavage and can initiate reactions on new DNA molecules as long as free HsdR molecules are available. In contrast, the MTase of EcoR124I does not turnover and additional cleavage of circular DNA is not observed by inclusion of RecBCD, a helicase-nuclease that degrades the linear DNA product resulting from Type I cleavage. Roles for Type I restriction endonuclease subunit dynamics in restriction alleviation in the cell are discussed.
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Registered trials
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