ReviewBiochemical Society transactions2011
Translocation, switching and gating: potential roles for ATP in long-range communication on DNA by Type III restriction endonucleases.
Review in Biochemical Society transactions, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
What it found
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Who cites it
11 citing papers in PubMed.
- Short-range translocation by a restriction enzyme motor triggers diffusion along DNA.Nature chemical biology · 2024Article
- Single-site DNA cleavage by Type III restriction endonuclease requires a site-bound enzyme and a trans-acting enzyme that are ATPase-activated.Nucleic acids research · 2018Article
- CgII cleaves DNA using a mechanism distinct from other ATP-dependent restriction endonucleases.Nucleic acids research · 2017Article
- Re-evaluating the kinetics of ATP hydrolysis during initiation of DNA sliding by Type III restriction enzymes.Nucleic acids research · 2015Article
- Type III restriction-modification enzymes: a historical perspective.Nucleic acids research · 2014Review
- Highlights of the DNA cutters: a short history of the restriction enzymes.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
- Structural insights into the assembly and shape of Type III restriction-modification (R-M) EcoP15I complex by small-angle X-ray scattering.Journal of molecular biology · 2012Article
- ZRANB3 is a structure-specific ATP-dependent endonuclease involved in replication stress response.Genes & development · 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
- Characterization of type II and III restriction-modification systems from Bacillus cereus strains ATCC 10987 and ATCC 14579.Journal of bacteriology · 2012Article
Corrections and comments
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Authors and funding
1 author.
Funding
Abstract
To cleave DNA, the Type III RM (restriction-modification) enzymes must communicate the relative orientation of two recognition sequences, which may be separated by many thousands of base pairs. This long-range interaction requires ATP hydrolysis by a helicase domain, and both active (DNA translocation) and passive (DNA sliding) modes of motion along DNA have been proposed. Potential roles for ATP binding and hydrolysis by the helicase domains are discussed, with a focus on bipartite ATPases that act as molecular switches.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.