Interdomain communication in the endonuclease/motor subunit of type I restriction-modification enzyme EcoR124I
Language English Country Germany Media print-electronic
Document type Journal Article, Research Support, Non-U.S. Gov't, Research Support, U.S. Gov't, Non-P.H.S.
- MeSH
- Adenosine Triphosphate chemistry metabolism MeSH
- Amino Acid Motifs MeSH
- DNA chemistry metabolism MeSH
- Phenotype MeSH
- Genotype MeSH
- Hydrolysis MeSH
- Catalysis MeSH
- Kinetics MeSH
- Conserved Sequence MeSH
- Quantum Theory MeSH
- Lysine MeSH
- Mutation MeSH
- Mutagenesis, Site-Directed MeSH
- Deoxyribonucleases, Type I Site-Specific chemistry genetics metabolism MeSH
- Molecular Dynamics Simulation MeSH
- Protein Structure, Tertiary MeSH
- Protein Binding MeSH
- Binding Sites MeSH
- Structure-Activity Relationship MeSH
- Publication type
- Journal Article MeSH
- Research Support, Non-U.S. Gov't MeSH
- Research Support, U.S. Gov't, Non-P.H.S. MeSH
- Names of Substances
- Adenosine Triphosphate MeSH
- DNA MeSH
- endodeoxyribonuclease EcoR124I MeSH Browser
- Lysine MeSH
- Deoxyribonucleases, Type I Site-Specific MeSH
Restriction-modification systems protect bacteria from foreign DNA. Type I restriction-modification enzymes are multifunctional heteromeric complexes with DNA-cleavage and ATP-dependent DNA translocation activities located on endonuclease/motor subunit HsdR. The recent structure of the first intact motor subunit of the type I restriction enzyme from plasmid EcoR124I suggested a mechanism by which stalled translocation triggers DNA cleavage via a lysine residue on the endonuclease domain that contacts ATP bound between the two helicase domains. In the present work, molecular dynamics simulations are used to explore this proposal. Molecular dynamics simulations suggest that the Lys-ATP contact alternates with a contact with a nearby loop housing the conserved QxxxY motif that had been implicated in DNA cleavage. This model is tested here using in vivo and in vitro experiments. The results indicate how local interactions are transduced to domain motions within the endonuclease/motor subunit.
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