Processive translocation and DNA unwinding by individual RecBCD enzyme molecules
Explore this paper's citation graph
Summary
It is shown that unwinding is both continuous and processive, occurring at a maximum rate of 972 ± 172 base pairs per second, with as many as 42,300 base pairs of dsDNA unwound by a single RecBCD enzyme molecule.
- Type
- article
- Published
- 2001-01-18
- Cited by
- 340
- References
- 46
- OpenAlex
- https://openalex.org/W1503666504
- Semantic Scholar
- https://api.semanticscholar.org/CorpusID:4399125
Keywords
RecBCD, Helicase, DNA, Biophysics, Base pair
References
- Escherichia coli RecBCD enzyme: inducible overproduction and reconstitution of the ATP-dependent deoxyribonuclease from purified subunits.
- Protamine-induced condensation and decondensation of the same DNA molecule.
- Processivity of the DNA helicase activity of Escherichia coli recBCD enzyme.
- Microtubule movement by a biotinated kinesin bound to streptavidin-coated surface.
- Translocation step size and mechanism of the RecBC DNA helicase
- On the role of ATP in phosphodiester bond hydrolysis catalyzed by the recBC deoxyribonuclease of Escherichia coli.
- Biotination of proteins in vivo. A post-translational modification to label, purify, and study proteins.
- Single-molecule studies of the effect of template tension on T7 DNA polymerase activity
- The genetic dependence of recombination in recD mutants of Escherichia coli.
- Chi‐activated RecBCD enzyme possesses 5′→3′ nucleolytic activity, but RecBC enzyme does not: evidence suggesting that the alteration induced by Chi is not simply ejection of the RecD subunit
- Transcription by single molecules of RNA polymerase observed by light microscopy
- Reversible inactivation of the Escherichia coli RecBCD enzyme by the recombination hotspot chi in vitro: evidence for functional inactivation or loss of the RecD subunit.
- The recombination hotspot χ is a regulatory sequence that acts by attenuating the nuclease activity of the E. coli RecBCD enzyme
- Substrate specificity of the DNA unwinding activity of the RecBC enzyme of Escherichia coli.
- RecBC enzyme nicking at Chi sites during DNA unwinding: location and orientation-dependence of the cutting.
- The recombination hot spot chi activates RecBCD recombination by converting Escherichia coli to a recD mutant phenocopy.
- Differences in the chemical reactivity of individual molecules of an enzyme
- The mutant recBCD enzyme, recB2109CD enzyme, has helicase activity but does not promote efficient joint molecule formation in vitro.
- A model for the mechanism of polymerase translocation.
- Interaction with the recombination hot spot chi in vivo converts the RecBCD enzyme of Escherichia coli into a chi-independent recombinase by inactivation of the RecD subunit.
Cited by
- Single-molecule studies of complex systems: the replisome.
- Real-time direct observation of single-molecule DNA hydrolysis by exonucleaseIII
- Mobility analysis of super-resolved proteins on optically stretched DNA: comparing imaging techniques and parameters.
- Sequence-dependent nanometer-scale conformational dynamics of individual RecBCD–DNA complexes
- Integrating single-molecule visualization and DNA micromanipulation
- Single-Molecule Investigations of Enzyme Dynamics: RecBCD Helicase Motion and glmS Ribozyme Cleavage
- Kinetics of Motor Protein Translocation on Single Stranded DNA
- DNA curtains: novel tools for imaging protein-nucleic acid interactions at the single-molecule level.
- Single-molecule and single-particle imaging of molecular motors in vitro and in vivo.
- Structure and Mechanisms of SF2 DNA Helicases.
- Overview: what are helicases?
- Fluorescence and labelling: how to choose and what to do.
- Orf protein modulates phage and bacterial pathways of genetic recombination
- The fluorescence properties and binding mechanism of SYTOX green, a bright, low photo-damage DNA intercalating agent
- Ten years of tension: single-molecule DNA
- DNA Helicases and DNA Motor Proteins
- Fluorescent Methods for Molecular Motors
- PURIFICATION AND CHARACTERIZATION OF THE RECD PROTEIN-HOMOLOGUE FROM DEINOCOCCUS RADIODURANS
- Identification of pre-synaptic processing proteins from bacteroides fragilis
- Optical diffraction-based silicon sensors for the detection of DNA sequences
Related papers
- RecBCD enzyme is a bipolar DNA helicase
- Small-molecule sensitization of RecBCD helicase-nuclease to a Chi hotspot-activated state
- Monitoring the Individual Motor Activities of RecB and RecD within the E.coli Recbcd Helicase
- Small-molecule sensitization of RecBCD helicase–nuclease to a Chi hotspot-activated state
- RecBCD enzyme is a DNA helicase with fast and slow motors of opposite polarity
- Direct observation of RecBCD helicase as single-stranded DNA translocases.
- Intersubunit signaling in RecBCD enzyme, a complex protein machine regulated by Chi hot spots.
- Direct Observation of Recbcd Helicase as ssDNA Translocases
- A model of DNA unwinding dynamics by the RecBCD complex and its regulation by Chi recognition.