This stimulation likely plays a role in DNA strand and protein displacement by UvrD in nucleotide excision repair. Promotion of UvrD-catalyzed unwinding of nicked

2012-03-09

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.

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. 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- assembly or interaction with an accessory protein is needed to activate its helicase activity in vitro. 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. 2020-10-23 · UvrD, also termed Helicase II, binds directly to RNAP and is proposed to function within the TCR by using its inherent ATPase activity for backtracking the stalled RNAP without displacing it 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.

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.

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

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. IMPORTANCE Biofilm development is a key component of the ability of Pseudomonas aeruginosa to evade host immune defenses and resist multiple drugs.

1988-04-01

subtilis . Below, we review the functions of UvrD, Rep and PcrA and their potential roles in conflict avoidance. 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.

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. 2003-01-31 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 For the XPD helicase in eukaryotic NER a similar function in analogy to UvrB has been proposed, whereas XPB the second helicase uses only its ATPase activity during eukaryotic NER. In prokaryotic mismatch repair (MMR) UvrD again plays a central role. 2010-07-09 1997-01-17 2009-04-03 2015-04-17 However, there have been conflicting reports about the oligomeric state of the active helicase in vitro, some claiming that a UvrD monomer can function as a processive helicase 36,37, whereas In conclusion, our data show that the lethality in rep uvrD mutants is not a result of the overlapping functions of both helicases.
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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.

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.
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To define further the role of UvrD in DNA repair a site-specific mutant was characterized. The mutation, uvrDQ251E, resides within helicase motif III, a conserved

Below, we review the functions of UvrD, Rep and PcrA and their potential roles in conflict avoidance. 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.

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2006-08-01

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.

However, there have been conflicting reports about the oligomeric state of the active helicase in vitro, some claiming that a UvrD monomer can function as a processive helicase 36,37, whereas

The UvrD helicase proves therefore to play a new role, unrelated to DNA melting, in vivo. John Atkinson, Colin P. Guy, Chris J. Cadman, Geri F. Moolenaar, Nora Goosen, Peter McGlynn #=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. #=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 UvrD-like DNA helicase C-terminal domain profile. IPR014017: UvrD-like DNA helicase, C-terminal 289 566 25.557 Pfam PF00580 UvrD/REP helicase N-terminal domain IPR034739: UvrD/AddA helicase, N-terminal 12 273 6.4E-74 Gene3D G3DSA:1.10.486.10 384 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 Has both ATPase and helicase activities. Unwinds DNA duplexes with 3' to 5' polarity with respect to the bound strand and initiates unwinding most effectively when a single-stranded region is present. Involved in the post-incision events of nucleotide excision repair and … 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.

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.