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The Helicase-Like Domains of Type III Restriction Enzymes Trigger Long-Range Diffusion Along DNA
- Source :
- Science. 340:353-356
- Publication Year :
- 2013
- Publisher :
- American Association for the Advancement of Science (AAAS), 2013.
-
Abstract
- Sliding Restriction Helicase enzymes access the genetic information stored in double-helical DNA and RNA by opening the individual strands. Pseudo-helicases, including bacterial Type III restriction enzymes, use adenosine triphosphate (ATP) hydrolysis to communicate between two distant restriction sites on the same DNA and excise it only if the DNA is sensed as “foreign.” Schwarz et al. (p. 353 ) show that the bacterial Type III restriction enzyme, EcoP15I, undergoes an ATP-dependent conformational switch that promotes sliding along the DNA to allow the enzyme to localize to its target.
- Subjects :
- DNA polymerase
DNA polymerase II
Article
03 medical and health sciences
Adenosine Triphosphate
0302 clinical medicine
DNA Cleavage
030304 developmental biology
chemistry.chemical_classification
0303 health sciences
DNA ligase
Multidisciplinary
DNA clamp
biology
Hydrolysis
DNA Helicases
Helicase
DNA
Protein Structure, Tertiary
DNA binding site
Microscopy, Fluorescence
Biochemistry
chemistry
biology.protein
Nucleic Acid Conformation
DNA supercoil
Primase
Deoxyribonucleases, Type III Site-Specific
030217 neurology & neurosurgery
Subjects
Details
- ISSN :
- 10959203 and 00368075
- Volume :
- 340
- Database :
- OpenAIRE
- Journal :
- Science
- Accession number :
- edsair.doi.dedup.....d3ca2e3b102c8e1aed254291922a032b