Type III restriction-modification enzymes: a historical perspective
Open Access
- 17 July 2013
- journal article
- review article
- Published by Oxford University Press (OUP) in Nucleic Acids Research
- Vol. 42 (1), 45-55
- https://doi.org/10.1093/nar/gkt616
Abstract
Restriction endonucleases interact with DNA at specific sites leading to cleavage of DNA. Bacterial DNA is protected from restriction endonuclease cleavage by modifying the DNA using a DNA methyltransferase. Based on their molecular structure, sequence recognition, cleavage position and cofactor requirements, restriction–modification (R–M) systems are classified into four groups. Type III R–M enzymes need to interact with two separate unmethylated DNA sequences in inversely repeated head-to-head orientations for efficient cleavage to occur at a defined location (25–27 bp downstream of one of the recognition sites). Like the Type I R–M enzymes, Type III R–M enzymes possess a sequence-specific ATPase activity for DNA cleavage. ATP hydrolysis is required for the long-distance communication between the sites before cleavage. Different models, based on 1D diffusion and/or 3D-DNA looping, exist to explain how the long-distance interaction between the two recognition sites takes place. Type III R–M systems are found in most sequenced bacteria. Genome sequencing of many pathogenic bacteria also shows the presence of a number of phase-variable Type III R–M systems, which play a role in virulence. A growing number of these enzymes are being subjected to biochemical and genetic studies, which, when combined with ongoing structural analyses, promise to provide details for mechanisms of DNA recognition and catalysis.Keywords
This publication has 82 references indexed in Scilit:
- Type III restriction endonuclease EcoP15I is a heterotrimeric complex containing one Res subunit with several DNA-binding regions and ATPase activityNucleic Acids Research, 2011
- Translocation, switching and gating: potential roles for ATP in long-range communication on DNA by Type III restriction endonucleasesBiochemical Society Transactions, 2011
- DNA translocation by type III restriction enzymes: a comparison of current models of their operation derived from ensemble and single-molecule measurementsNucleic Acids Research, 2011
- Type III restriction enzymes cleave DNA by long-range interaction between sites in both head-to-head and tail-to-tail inverted repeatProceedings of the National Academy of Sciences of the United States of America, 2010
- Phasevarions Mediate Random Switching of Gene Expression in Pathogenic NeisseriaPLoS Pathogens, 2009
- Type III restriction enzymes communicate in 1D without looping between their target sitesProceedings of the National Academy of Sciences of the United States of America, 2009
- Fast-scan atomic force microscopy reveals that the type III restriction enzyme EcoP15I is capable of DNA translocation and loopingProceedings of the National Academy of Sciences of the United States of America, 2007
- DNA looping and translocation provide an optimal cleavage mechanism for the type III restriction enzymesThe EMBO Journal, 2007
- Type III DNA restriction and modification systems EcoP1 and EcoP15: Nucleotide sequence of the EcoP1 operon, the EcoP15mod gene and some EcoP1mod mutantsJournal of Molecular Biology, 1988
- Cleavage and methylation of DNA by the restriction endonuclease HinfIII isolated from Haemophilus influenzae RfJournal of Molecular Biology, 1980