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The HRDC domain of E. coli RecQ helicase controls single-stranded DNA translocation and double-stranded DNA unwinding rates without affecting mechanoenzymatic coupling
- Source :
- Scientific Reports
- Publication Year :
- 2015
- Publisher :
- Springer Science and Business Media LLC, 2015.
-
Abstract
- DNA-restructuring activities of RecQ-family helicases play key roles in genome maintenance. These activities, driven by two tandem RecA-like core domains, are thought to be controlled by accessory DNA-binding elements including the helicase-and-RnaseD-C-terminal (HRDC) domain. The HRDC domain of human Bloom’s syndrome (BLM) helicase was shown to interact with the RecA core, raising the possibility that it may affect the coupling between ATP hydrolysis, translocation along single-stranded (ss)DNA and/or unwinding of double-stranded (ds)DNA. Here, we determined how these activities are affected by the abolition of the ssDNA interaction of the HRDC domain or the deletion of the entire domain in E. coli RecQ helicase. Our data show that the HRDC domain suppresses the rate of DNA-activated ATPase activity in parallel with those of ssDNA translocation and dsDNA unwinding, regardless of the ssDNA binding capability of this domain. The HRDC domain does not affect either the processivity of ssDNA translocation or the tight coupling between the ATPase, translocation and unwinding activities. Thus, the mechanochemical coupling of E. coli RecQ appears to be independent of HRDC-ssDNA and HRDC-RecA core interactions, which may play roles in more specialized functions of the enzyme.
- Subjects :
- DNA, Bacterial
RecQ helicase
DNA, Single-Stranded
Chromosomal translocation
medicine.disease_cause
Article
03 medical and health sciences
chemistry.chemical_compound
0302 clinical medicine
ATP hydrolysis
Enzyme Stability
Escherichia coli
medicine
Humans
030304 developmental biology
0303 health sciences
Multidisciplinary
RecQ Helicases
biology
Helicase
Processivity
Protein Structure, Tertiary
Cell biology
Rec A Recombinases
enzymes and coenzymes (carbohydrates)
Biochemistry
chemistry
biology.protein
030217 neurology & neurosurgery
DNA
Subjects
Details
- ISSN :
- 20452322
- Volume :
- 5
- Database :
- OpenAIRE
- Journal :
- Scientific Reports
- Accession number :
- edsair.doi.dedup.....a519d2427b18276bb655a24bed945eb2