UvrD is a DNA-dependent ATPase and helicase that belongs to the helicase SF1 superfamily and catalyzes the unwinding of duplex DNA in a 3' to 5' direction.[1]

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

In this study, the func-tional characterization of UvrD helicase from Haemophilus inﬂuenzae and Helicobacter pylori is reported. 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 2012-03-09 · The Escherichia coli UvrD helicase is known to function in the mismatch repair and nucleotide excision repair pathways and has also been suggested to have roles in recombination and replication restart. 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

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. 6). The specific role of

#=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.

2006-08-01

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.

2020-10-23

DNA helicases are motor proteins that function to unwind duplex (ds) DNA during DNA replication, recombination, and repair and are also 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 gene was cloned, and a histidine-tagged form of the protein was expressed and purified to 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 UvrD-like helicase ATP-binding PROSITE-ProRule annotation. Add BLAST: 282: Domain i: 291 – 568: UvrD-like helicase C-terminal PROSITE-ProRule annotation. Add BLAST: 278 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.

1 Publication 2018-10-19 · MutL functions as a processivity factor for UvrD helicase activity.
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#=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. 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.
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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).

Escherichia coli UvrD is a non-hexameric SF1 helicase and ssDNA translocase that functions in methyl-directed mismatch repair7 and nucleotide excision repair8 of DNA, reversal of replication forks9,10 and replication of some plasmids.11 UvrD also functions to remove proteins from DNA12,13 and as an anti-recombinase by displacing RecA Feb 4, 2017 Abstract. The PcrA/UvrD helicase functions in multiple pathways that promote bacterial genome stability including the suppression of conflicts Apr 17, 2018 An exemplary Escherichia coli helicase, UvrD, belonging to SF1, has many cellular roles such as methyl-directed mismatch repair (Iyer et al., 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 UvrD is a DNA-dependent ATPase and helicase that belongs to the helicase SF1 superfamily and catalyzes the unwinding of duplex DNA in a 3' to 5' direction.[1] 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 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 The DNA helicase UvrD (helicase II) protein plays an important role in nucleotide excision repair, mismatch repair, rolling circular plasmid replication, The Rep family helicases are composed of four structural domains. 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.