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View protein in PROSITE PS51198, UVRD_HELICASE_ATP_BIND, 1 hit PS51217, UVRD_HELICASE_CTER,

This section displays by default the canonical protein sequence and upon request all isoforms described in the entry.

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).

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 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 … 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.

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.

2017-02-04

Moreover, although UvrAB can promote limited strand displacement, stimulation of UvrD did not require the strand displacement function of UvrAB. We conclude that UvrAB, like MutL, modulate UvrD helicase activity. Escherichia coli UvrD is a superfamily 1 DNA helicase and single-stranded DNA (ssDNA) translocase that functions in DNA repair and plasmid replication and as an anti-recombinase by removing RecA protein from ssDNA. UvrD couples ATP binding and hydrolysis to unwind double-stranded DNA and translocate along ssDNA with 3'-to-5' directionality.

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.

Accessory helicases in E. coli. It has putative helicase carrying an UvrD-like helicase C-terminal domain, and two contiguous putative serine/threonine protein kinases (Fig.

Therefore, helicase assays were carried out using fixed concentration (40 n m ) of HiUvrD or HpUvrD and different DNA structures (Table S2, structures 1–9; 1 n m each), which were used in the DNA‐binding studies. 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, 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 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).
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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. 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.

#=GF GA 23.00 23.00; #=GF TC 23.00 23.00; #=GF NC 22.90 22.90; #=GF BM hmmbuild HMM.ann SEED.ann #=GF SM hmmsearch -Z 47079205 -E 1000 --cpu 4 HMM pfamseq #=GF TP Domain #=GF RC Structure of Swiss:P09980 #=GF RN [1] #=GF RM 9288744 #=GF RT Major domain swiveling revealed by the crystal structures of #=GF RT complexes of E. coli Rep helicase 2009-04-03 · The stimulation is specific for UvrD, as UvrAB failed to stimulate Rep helicase, a UvrD homologue.
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In conclusion, our data show that the lethality in rep uvrD mutants is not a result of the overlapping functions of both helicases. UvrD, but not Rep, plays a role of RecA nucleoprotein filament remover in E. coli. The UvrD helicase proves therefore to play a new role, unrelated to DNA melting, in vivo.

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. 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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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.

The UvrD helicase proves therefore to play a new role, unrelated to DNA melting, in vivo. UvrD is an abundant helicase in Escherichia coli with well characterized functions in mismatch and nucleotide excision repair and a possible role in displacement of proteins such as RecA from UvrD exhibits modest processivity as a DNA helicase (40–50 bp) (53– 55) making this protein an interesting choice for the helicase responsible for the unwinding event in MMR. UvrD is also the helicase responsible for the unwinding event associated with excision repair ( 56 – 59 ), which requires unwinding of a short 12–13 base long oligonucleotide well within the limits of the The closed conformation activates the helicase, but it can also generate super-helicases capable of unzipping long stretches of DNA at high speed and with considerable force. Comstock et al. used optical tweezers and fluorescence microscopy to simultaneously measure the structure and function of the bacterial helicase UvrD. Structures of UvrD-like SF1 helicase solved so far share a four-subdomain tertiary arrangement (1A/2A/1B/2B) (Singleton et al., 2007), including two RecA-like domains (1A/2A) which contain the ATP binding site and are proposed to function as the translocase (Dillingham et al., 2001; Lee and Yang, 2006), and a flexible domain (2B) which is believed to play a regulatory role in helicase activity #=GF ID UvrD-helicase #=GF AC PF00580.22 #=GF DE UvrD/REP helicase N-terminal domain #=GF AU Bateman A;0000-0002-6982-4660 #=GF SE MRC-LMB Genome group.