recQ Antibody, FITC conjugated

1. To illustrate the single-molecule unwinding assay and the analysis routine, we provide DNA unwinding measurements of Escherichia coli RecQ helicase under a variety of conditions (Na+, ATP, temperature, and DNA substrate geometry). PMID: 27131595
2. Data show that the single-stranded DNA binding protein (SSB)-RecQ helicase (RecQ) interaction changes the binding mode of SSB, thereby allowing RecQ to gain access to ssDNA and facilitating DNA unwinding. PMID: 29059328
3. 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. PMID: 26067769
4. Thus, bacterial type 1A topos maintain the stability of the genome (i) by preventing over-replication originating from oriC (topo I alone) and R-loops and (ii) by acting with RecQ. PMID: 25102178
5. The study found that the interaction of RecQ with DNA results in a drastic acceleration of the rate-limiting ATP cleavage step, which occurs productively due to subsequent rapid phosphate release. PMID: 25539922
6. The results shed light on the nature of conformational changes leading to processive ssDNA translocation and multistranded DNA processing by RecQ helicases. PMID: 24403069
7. Results describe the mechanism of DNA unwinding by the Escherichia coli RecQ helicase using a new sensitive helicase assay based on fluorescence cross-correlation spectroscopy (FCCS) with two-photon excitation. PMID: 20048388
8. The aromatic-rich loop in RecQ is critical for coupling ATPase and DNA-binding/unwinding activities. PMID: 16340008
9. E.coli RecQ functions as a monomer and some of the Superfamily 2 helicases may function through an "inchworm" mechanism PMID: 16507576
10. RecQ promotes the net accumulation of bimolecular recombination intermediates in vivo, indicating a second paradigm for the in vivo effect of RecQ-like proteins. PMID: 17466628
11. SSB is a broadly conserved RecQ-binding protein PMID: 17483090
12. These results support a model in which RecQ has evolved an SSB-C-terminal binding site on its winged-helix domain as an adaptation that aids its cellular functions on SSB/DNA nucleoprotein substrates. PMID: 19150358

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KEGG: ecj:JW5855

STRING: 316385.ECDH10B_4013