Why is it important? Function Primary Structure Secondary Structure Tertiary Structure DNA Replication Summary of Structural Article References. Contributors.
1988-04-01 · CPX-5542, MutL-UvrD DNA helicase complex: DIP i: DIP-11103N: IntAct i: P03018, 39 interactors: STRING i: 511145.b3813
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doi: 10.1016/j.cell.2006.10.049. Authors Jae Young Lee 1 , Wei Yang. 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.
Contributors.
>tr|A0T0Q4|A0T0Q4_THAPS DNA replication helicase OS=Thalassiosira pseudonana >tr|B8C0C4|B8C0C4_THAPS UVRD/Rep like helicase (Fragment)
PubMed: 33097771 Search on PubMed Search on PubMed Central; DOI: 10.1038/s42003-020-01332-2; Primary Citation of Related Structures: 6YI2, 6YHZ; PubMed Abstract: Tte Uvrd Helicase, supplied by New England Biolabs, used in various techniques. Bioz Stars score: 94/100, based on 0 PubMed citations.
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 …
Previously, we have developed an isothermal DNA amplification method using the UvrD helicase from E coli (1). Unlike the polymerase chain reaction (PCR) that is depend- The helicase activity of the Tte-UvrD is described, as are the effects of the Tte-MutL protein on unwinding reactions catalyzed by Tte-UvrD helicase.
(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.
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UvrD helicase plays essential roles in multiple DNA metabolic processes, including methyl-directed mismatch repair. UvrD monomers can translocate along single-stranded DNA, but self-assembly or interaction with an accessory factor is required to activate processive DNA unwinding in vitro. 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.
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. 16 Oct 2013 UvrD-like helicases play diverse roles in DNA replication, repair and recombination pathways. An emerging body of evidence suggests that
19 Oct 2018 MutL functions as a processivity factor for UvrD helicase activity. Abstract.
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Tte UvrD Helicase is a repair helicase capable of unwinding double-stranded DNA, without a requirement for a specific flap or overhang structure, from the thermophilic organism Thermoanaerobacter tengcongensis.It is active on a wide range of DNA substrates and, along with its thermostability (active to 70°C), Tte UvrD Helicase has been demonstrated to be a useful additive for improving
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.
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UvrD helicase plays essential roles in multiple DNA metabolic processes, including methyl-directed mismatch repair. UvrD monomers can translocate along single-stranded DNA, but self-assembly or interaction with an accessory factor is required to activate processive DNA unwinding in vitro.
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 … 2019-08-13 2017-11-14 Veaute, X. et al. UvrD helicase, unlike Rep helicase, dismantles RecA nucleoprotein filaments in Escherichia coli.