Key Publications University of Gothenburg

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Replikation – transkriptionskonflikter i bakterier - naturen

UvrD is known to load at single-stranded/ double-stranded junctions and, depending on its oligmeric state, translocate on single-stranded DNA as a monomer or unwind duplex DNA as a dimer.3 Therefore, the assembly state of UvrD as it pulls RNA polymerase backward is of 2010-07-09 2012-03-09 2017-02-04 2020-10-23 1988-04-01 UvrD is a DNA helicase that participates in nucleotide excision repair and several replication-associated processes, including methyl-directed mismatch repair and recombination. UvrD is capable of displacing oligonucleotides from synthetic forked DNA structures in vitro and is essential for viability in the absence of Rep, a helicase associated with processing replication forks. 2019-08-13 UvrD (DNA helicase II) has been implicated in DNA replication, DNA recombination, nucleotide excision repair, and methyl-directed mismatch repair. The enzymatic function of UvrD is to translocate along a DNA strand in a 3' to 5' direction and unwind duplex DNA utilizing a DNA-dependent ATPase activity.

Uvrd helicase function

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To test whether the helicase function of UvrD is required for replication fork reversal, we used a previously characterized mutation in the helicase motif IV of the chromosomal uvrD gene (R284A). Escherichia coli UvrD is a superfamily 1 helicase/translocase that functions in DNA repair, replication, and recombination. Although a UvrD monomer can translocate along single-stranded DNA, self UvrD, a ubiquitous bacterial helicase that plays important roles in multiple DNA metabolic pathways, is essential for genome stability and might, therefore, be crucial in bacterial physiology and pathogenesis. In this study, the functional characterization of UvrD helicase from Haemophilus influenzae and Helicobacter pylori is reported. Abstract. The PcrA/UvrD helicase functions in multiple pathways that promote bacterial genome stability including the suppression of conflicts between replication and transcription and facilitating the repair of transcribed DNA. 2012-05-09 · Translocation of UvrD. UvrD is a helicase and translocase that functions in excision repair to remove the damaged segment of DNA so that DNA polymerase can fill in the gap.

tr B3KYW5 B3KYW5_PLAKH SICA antigen Fragment OS

The primary intermediate DNA structure in these two processes is the Holliday junction. 1988-04-01 · Strongly sensitive to UV, ciprofloxacin (CFX), and azidothymidine (AZT) in single deletion mutants, radA-uvrD double deletions are more sensitive yet.

Uvrd helicase function

tr B3KYW5 B3KYW5_PLAKH SICA antigen Fragment OS

Uvrd helicase function

This domain is also found in subunit AddA of bacterial helicase-nuclease complex AddAB. The AddA subunit is the one responsible for the helicase activity [ (PUBMED:21071401) ]. This entry represents the ATP-binding domain found in UvrD-like and AddA helicases. GO function: This report consolidates knowledge on the new role of UvrD in filamentous phage replication, a function previously thought to be exclusive of Rep helicase.

The enzymatic function of UvrD is to translocate along a DNA strand in a 3' to 5' direction and unwind duplex DNA utilizing a DNA-dependent ATPase activity. In addition, UvrD interacts with many other UvrD is a DNA helicase that participates in nucleotide excision repair and several replication-associated processes, including methyl-directed mismatch repair and recombination. UvrD is capable of displacing oligonucleotides from synthetic forked DNA structures in vitro and is essential for viability in the absence of Rep, a helicase associated with processing replication forks. UvrD, a member of the helicase SF1 superfamily, plays an essential role in bacterial NER by unwinding the duplex DNA in the 3' to 5' direction to displace the lesion-containing strand. In order to achieve conditional control over NER, we generated a light-activated DNA helicase. uvrD homolog has been shown to partially compensate for the repair function of E. coli UvrD, suggesting that the function of the helicase is evolutionarily conserved (11). Characterization of this protein indicates that the T. thermophilus UvrD pos-sesses a 3-5 DNA helicase activity similar to the E. coli UvrD (12).
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The Rep family function as dimers. REP helicases catalyse ATP dependent unwinding of  Oct 18, 2017 Escherichia coli UvrD (EcUvrD) helicase plays a crucial role in nucleotide excision repair, mismatch repair and in the regulation of homologous  Aug 13, 2019 Escherichia coli UvrD is a superfamily 1 helicase/translocase that functions in DNA repair, replication, and recombination. Although a UvrD  An interesting example is provided by the UvrD helicase (also annotated Helicase II, or PcrA in many gram positive bacteria including Bacillus subtilis) which has  Reference, Petit MA, Dervyn E, Rose M, Entian KD, McGovern S, Ehrlich SD, Bruand C. PcrA is an essential DNA helicase of Bacillus subtilis fulfilling functions   Mar 12, 2019 The UvrD protein or Helicase II is a member of helicase Superfamily 1 and functions in methyl-directed mismatch and nucleotide excision repair  Apr 17, 2015 Chemla's lab team looked at the structure-function relationship in the helicase UvrD, a protein, found in the bacterium E. coli, that separates  Apr 17, 2015 used optical tweezers and fluorescence microscopy to simultaneously measure the structure and function of the bacterial helicase UvrD. They  Jun 9, 2010 Helicases and nucleic acids offer simple motor systems for extensive Lessons Learned from UvrD Helicase: Mechanism for Directional Movement of two-state folding, calculated as a function of cavity radius according Nov 19, 2013 Structure and Function Measurements 46.

Characterization of this protein indicates that the T. thermophilus UvrD pos-sesses a 3-5 DNA helicase activity similar to the E. coli UvrD (12). 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 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 specificity of isothermal amplification reactions, particularly in conjunction with the WarmStart® LAMP Kit (DNA & RNA). Workflow. Helicases are a class of enzymes vital to all organisms. Their main function is to unpack an organism's genes.
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Uvrd helicase function

UvrD (DNA helicase II) has been implicated in DNA replication, DNA recombination, nucleotide excision repair, and methyl-directed mismatch repair. The enzymatic function of UvrD is to translocate along a DNA strand in a 3' to 5' direction and unwind duplex DNA utilizing a DNA-dependent ATPase activity. In addition, UvrD interacts with many other UvrD is a DNA helicase that participates in nucleotide excision repair and several replication-associated processes, including methyl-directed mismatch repair and recombination. UvrD is capable of displacing oligonucleotides from synthetic forked DNA structures in vitro and is essential for viability in the absence of Rep, a helicase associated with processing replication forks. UvrD, a member of the helicase SF1 superfamily, plays an essential role in bacterial NER by unwinding the duplex DNA in the 3' to 5' direction to displace the lesion-containing strand.

Characterization of this protein indicates that the T. thermophilus UvrD pos-sesses a 3-5 DNA helicase activity similar to the E. coli UvrD … 2018-10-19 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 specificity of isothermal amplification reactions, particularly in conjunction with the WarmStart® LAMP Kit (DNA & … Bacterial UvrD helicase. 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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tr B3KYW5 B3KYW5_PLAKH SICA antigen Fragment OS

They are motor proteins that move directionally along a nucleic acid phosphodiester backbone, separating two annealed nucleic acid strands such as DNA and RNA (hence helic-+ -ase), using energy from ATP hydrolysis. The PcrA/UvrD helicase functions in multiple path-ways that promote bacterial genome stability includ-ing the suppression of conflicts between replication and transcription and facilitating the repair of tran-scribed DNA. The reported ability of PcrA/UvrD to bind and backtrack RNA polymerase (1,2) might be Escherichia coli UvrD DNA helicase functions in several DNA repair processes. As a monomer, UvrD can translocate rapidly and proc-essively along ssDNA; however, the monomer is a poor helicase. To unwind duplex DNA in vitro, UvrD needs to be activated either by self-assembly to form a dimer or by interaction with an acces-sory protein. UvrD, a member of the helicase SF1 superfamily, plays an essential role in bacterial NER by unwinding the duplex DNA in the 3' to 5' direction to displace the lesion-containing strand. In order to achieve conditional control over NER, we generated a light-activated DNA helicase.


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Characterization of this protein indicates that the T. thermophilus UvrD pos-sesses a 3-5 DNA helicase activity similar to the E. coli UvrD (12). 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 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 specificity of isothermal amplification reactions, particularly in conjunction with the WarmStart® LAMP Kit (DNA & RNA).

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UvrD Helicase 47. UvrD Helicase 01:04:  Mar 15, 2021 The PcrA/UvrD helicase binds directly to RNA polymerase (RNAP) but the structural basis for this interaction and its functional significance  Feb 27, 2020 A role for a DNA helicase in this capacity was first suggested by experimental evidence that UvrD unwinds stable DNA:RNA hybrids even more  Aug 30, 2018 Escherichia coli UvrD is a superfamily 1 helicase/translocase involved in Mechanistic insights into Lhr helicase function in DNA repair. UvrD helicase-RNA polymerase interactions are governed by UvrD's Function, and Can Transdifferentiate into Brown-like Adipocytes. 20, CLS10262, Y, Y, Y, Y, Y, Y, Y, 1, 1, 1, 1, 1, 1, 1, 1, 1, 1, D5-like helicase-primase 116, CLS10264, n, Y, n, Y, Y, Y, n, 1, 1, 1, 1, 2, 0, 0, 0, 0, 0, UvrD/REP helicase family protein protein of unknown function DUF305 conserved in bacteria. UvrD/REP helicase OS=Chloroflexus aurantiacus (strain ATCC 29366 / DSM >tr|A9WAY8|A9WAY8_CHLAA Cell envelope-related function transcriptional  Dna-directed rna polymerase 2 subunit, putative OS=Plasmodium knowlesi (strain function, putative OS=Plasmodium knowlesi (strain H) GN=PKH_072740 Helicase, belonging to UvrD family, putative OS=Plasmodium knowlesi (strain  Helicases are a class of enzymes vital to all organisms. their main function is to to the e.

UvrD Helicase 01:04:  Mar 15, 2021 The PcrA/UvrD helicase binds directly to RNA polymerase (RNAP) but the structural basis for this interaction and its functional significance  Feb 27, 2020 A role for a DNA helicase in this capacity was first suggested by experimental evidence that UvrD unwinds stable DNA:RNA hybrids even more  Aug 30, 2018 Escherichia coli UvrD is a superfamily 1 helicase/translocase involved in Mechanistic insights into Lhr helicase function in DNA repair.