2018-04-17

UvrD helicase, but not Rep helicase, efficiently disrupts RecA–ssDNA nucleoprotein filament. (A) RecA–ssDNA nucleoprotein filaments. (B) Preformed RecA–ssDNA complexes were incubated for 15 min with UvrD. The arrows point to the ssDNA covered with SSB. (C) Blow‐up of ssDNA covered with SSB.

Product Introduction Unwinds double-stranded DNA Thermostable to 65°C Reduces non-specific product UvrD monomers translocate in discrete steps with an average kinetic step-size, m=3.68 nt step(-1), a translocation rate constant, kt=51.3 steps s(-1), with a processivity corresponding to an average translocation distance of 2400 nt before dissociation PMID: 15561144; mutational analysis of a thermostable UvrD helicase PMID: 15955821 UniProtKB. x; UniProtKB. Protein knowledgebase. UniParc. Sequence archive. Help.

Characterization of a Thermostable UvrD Helicase and Its Participation in Helicase-dependent Amplification* Helicase-dependent amplification (HDA) is an isothermal in vitro DNA amplification method based upon the coordinated actions of helicases to separate double-stranded DNA and DNA polymerases to synthesize DNA. UvrD is a superfamily I DNA helicase with well documented roles in excision repair and methyl-directed mismatch repair (MMR) in addition to poorly understood roles in replication and recombination. The MutL protein is a homodimeric DNA-stimulated ATPase that plays a central role in MMR in Escherichia coli. UvrD is a helicase that is widely conserved in gram-negative bacteria. A uvrD homologue was identified in Mycobacterium tuberculosis on the basis of the homology of its encoded protein with Escherichia coli UvrD, with which it shares 39% amino acid identity, distributed throughout the protein. The helicase ac-tivity of the Tte-UvrD is described, as are the effects of the Tte-MutL protein on unwinding reactions catalyzed by Tte-UvrD helicase.

17 Apr 2018 An exemplary Escherichia coli helicase, UvrD, belonging to SF1, has many cellular roles such as methyl-directed mismatch repair (Iyer et al.,

Product Class: Other Tte UvrD Helicase Need assistance designing LAMP primers? Use the NEB LAMP Primer Design Tool. Product Introduction Unwinds double-stranded DNA Thermostable to 65°C Reduces non-specific product UvrD monomers translocate in discrete steps with an average kinetic step-size, m=3.68 nt step(-1), a translocation rate constant, kt=51.3 steps s(-1), with a processivity corresponding to an average translocation distance of 2400 nt before dissociation PMID: 15561144; mutational analysis of a thermostable UvrD helicase PMID: 15955821 UniProtKB. x; UniProtKB.

InterPro provides functional analysis of proteins by classifying them into families and predicting domains and important sites. We combine protein signatures from a number of member databases into a single searchable resource, capitalising on their individual strengths to produce a powerful integrated database and diagnostic tool.

4 Nov 2009 Hexameric helicases unwind DNA or RNA duplexes using ATP as an energy source. Watch and listen as James Berger and Nathan Thomsen Before DNA replication actually begins, a special type of enzyme called DNA helicase must move along the double-stranded DNA molecule and locate a region 20 Feb 2013 DNA helicases can melt base pairs using the energy released during the process of binding, hydrolysis and release of ATP. DNA helicase travels 5 Oct 2015 Learn about DNA helicase and the role it plays in starting the process of DNA replication.This lesson also covers information on how DNA The DNA helicase UvrD (helicase II) protein plays an important role in nucleotide excision repair, mismatch repair, rolling circular plasmid replication, UvrD helicase-RNA polymerase interactions are governed by UvrD's carboxy-terminal Tudor domain.

Affiliation 1 Laboratory of Molecular 2019-08-13 The helicase ac-tivity of the Tte-UvrD is described, as are the effects of the Tte-MutL protein on unwinding reactions catalyzed by Tte-UvrD helicase. Previously, we have developed an isothermal DNA amplification method using the UvrD helicase from E coli (1). … Helicase-dependent amplification (HDA) is an isothermal in vitro DNA amplification method based upon the coordinated actions of helicases to separate double-stranded DNA and DNA polymerases to synthesize DNA. Previously, a mesophilic form of HDA (mHDA) utilizing the Escherichia coli UvrD helicase, DNA polymerase I Klenow fragment, two accessory proteins, MutL and single-stranded DNA … 2012-03-09 UvrD helicase, but not Rep helicase, efficiently disrupts RecA–ssDNA nucleoprotein filament. (A) RecA–ssDNA nucleoprotein filaments. (B) Preformed RecA–ssDNA complexes were incubated for 15 min with UvrD. The arrows point to the ssDNA covered with SSB. (C) Blow‐up of ssDNA covered with SSB. Helicases use the energy derived from nucleoside triphosphate hydrolysis to unwind double helices in essentially every metabolic pathway involving nucleic acids. Earlier crystal structures have suggested that DNA helicases translocate along a single-stranded DNA in an inchworm fashion.
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It is involved in the post-incision events of nucleotide excision repair and methyl-directed mismatch repair. It unwinds DNA duplexes with 3'-5' polarity with respect to the bound strand and initiates unwinding most effectively when a single-stranded region is present.

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that UvrD can pull RNA polymerase backward suggests that the role of UvrD in both NER and collision avoidance is more complex than previously thought. For helicase aficionados, the subtle aspects of UvrD mechanism are intriguing. UvrD is known to load at single-stranded/ double-stranded junctions and, depending on its oligmeric state

Facebook gives people the power to As P. falciparum contains only one homologue of indicated that heliquinomycin isolated from the culture broth of UvrD helicase and human lacks this helicase, detailed studies Streptomyces sp. MJ1929-SF2 was able to inhibit DNA helicases including cloning and characterization of UvrD helicase of from HeLa cells (Chino et al., 1996). UvrD helicase-RNA polymerase interactions are governed by UvrD's carboxy-terminal Tudor domain. Kawale, A.A., Burmann, B.M. (2020) Commun Biol 3: 607-607.

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UvrD is a helicase that is widely conserved in gram-negative bacteria. A uvrD homologue was identified in Mycobacterium tuberculosis on the basis of the homology of its encoded protein with Escherichia coli UvrD, with which it shares 39% amino acid identity, distributed throughout the protein.

Unexpectedly, another prominent role for UvrD in NER 1988-04-01 UvrD helicase unwinds DNA one base pair at a time by a two-part power stroke Cell. 2006 Dec 29;127(7):1349-60.