ArticleJournal of molecular biology2008
The interrelationship of helicase and nuclease domains during DNA translocation by the molecular motor EcoR124I.
Article in Journal of molecular biology, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.
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Who cites it
15 citing papers in PubMed.
- 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 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
- The helical domain of the EcoR124I motor subunit participates in ATPase activity and dsDNA translocation.PeerJ · 2017Article
- Mapping DNA cleavage by the Type ISP restriction-modification enzymes following long-range communication between DNA sites in different orientations.Nucleic acids research · 2015Article
- Translocation-coupled DNA cleavage by the Type ISP restriction-modification enzymes.Nature chemical biology · 2015Article
- Functional coupling of duplex translocation to DNA cleavage in a type I restriction enzyme.PloS one · 2015Article
- ClpXP protease targets long-lived DNA translocation states of a helicase-like motor to cause restriction alleviation.Nucleic acids research · 2014Article
- Interdomain communication in the endonuclease/motor subunit of type I restriction-modification enzyme EcoR124I.Journal of molecular modeling · 2014Article
- Highlights of the DNA cutters: a short history of the restriction enzymes.Nucleic acids research · 2014Article
- Superfamily 2 helicases.Frontiers in bioscience (Landmark edition) · 2012Review
- Fluorescence methods to study DNA translocation and unwinding kinetics by nucleic acid motors.Methods in molecular biology (Clifton, N.J.) · 2012Article
- General and molecular microbiology and microbial genetics in the IM CAS.Journal of industrial microbiology & biotechnology · 2010Review
- Mutations altering a structurally conserved loop-helix-loop region of a viral packaging motor change DNA translocation velocity and processivity.The Journal of biological chemistry · 2010Article
- An Mrr-family nuclease motif in the single polypeptide restriction-modification enzyme LlaGI.Nucleic acids research · 2009Article
- 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.Nucleic acids research · 2009Article
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5 authors.
Funding
Abstract
The type I restriction-modification enzyme EcoR124I comprises three subunits with the stoichiometry HsdR2/HsdM2/HsdS1. The HsdR subunits are archetypical examples of the fusion between nuclease and helicase domains into a single polypeptide, a linkage that is found in a great many other DNA processing enzymes. To explore the interrelationship between these physically linked domains, we examined the DNA translocation properties of EcoR124I complexes in which the HsdR subunits had been mutated in the RecB-like nuclease motif II or III. We found that nuclease mutations can have multiple effects on DNA translocation despite being distinct from the helicase domain. In addition to reductions in DNA cleavage activity, we also observed decreased translocation and ATPase rates, different enzyme populations with different characteristic translocation rates, a tendency to stall during initiation and altered HsdR turnover dynamics. The significance of these observations to our understanding of domain interactions in molecular machines is discussed.
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