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Real-time observation of DNA translocation by the type I restriction modification enzyme EcoR124I
- Source :
- Nature structuralmolecular biology. 11(9)
- Publication Year :
- 2004
-
Abstract
- Type I restriction enzymes bind sequence-specifically to unmodified DNA and subsequently pull the adjacent DNA toward themselves. Cleavage then occurs remotely from the recognition site. The mechanism by which these members of the superfamily 2 (SF2) of helicases translocate DNA is largely unknown. We report the first single-molecule study of DNA translocation by the type I restriction enzyme EcoR124I. Mechanochemical parameters such as the translocation rate and processivity, and their dependence on force and ATP concentration, are presented. We show that the two motor subunits of EcoR124I work independently. By using torsionally constrained DNA molecules, we found that the enzyme tracks along the helical pitch of the DNA molecule. This assay may be directly applicable to investigating the tracking of other DNA-translocating motors along their DNA templates.
- Subjects :
- chemistry.chemical_classification
DNA ligase
DNA clamp
Binding Sites
Time Factors
biology
Base pair
DNA polymerase
Deoxyribonucleases, Type I Site-Specific
Biological Transport
Processivity
Nicking enzyme
DNA
Chromatin
Restriction enzyme
Protein Transport
Adenosine Triphosphate
Biochemistry
chemistry
Structural Biology
biology.protein
Biophysics
DNA supercoil
Molecular Biology
Plasmids
Subjects
Details
- ISSN :
- 15459993
- Volume :
- 11
- Issue :
- 9
- Database :
- OpenAIRE
- Journal :
- Nature structuralmolecular biology
- Accession number :
- edsair.doi.dedup.....fc02776208b0822ec8351064b0f1bc07