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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John Atkinson, Colin P. Guy, Chris J. Cadman, Geri F. Moolenaar, Nora Goosen, Peter McGlynn

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. Separation of the UvrD helicase and translocase activities is possible in vitro. 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 John Atkinson, Colin P. Guy, Chris J. Cadman, Geri F. Moolenaar, Nora Goosen, Peter McGlynn Gene References into Functions: Large domain movements upon UvrD dimerization and helicase activation has been reported.

Uvrd helicase function

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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. Helicases use the energy derived from nucleoside triphosphate hydrolysis to unwind double helices in essentially every metabolic pathway involving nucleic acids. Earlier crystal structures have suggested that DNA helicases translocate along a single-stranded DNA in an inchworm fashion.

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

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. 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 helicase function

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., 

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).

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.
Katarina widman

Uvrd helicase function

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.

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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2010-07-09

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.


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2017-02-04

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. Structure and Function Measure… 01: 04:33. 00:00/00:00. 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.

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.

1 Publication 2018-10-19 · MutL functions as a processivity factor for UvrD helicase activity. UvrD (DNA helicase II) has been implicated in DNA replication, DNA recombination, nucleotide excision repair, and methyl-directed mismatch repair.

Earlier crystal structures have suggested that DNA helicases translocate along a single-stranded DNA in an inchworm fashion. We report here a series of crystal structures of the UvrD helicase complexed with DNA and 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 2007-03-01 2018-04-17 PDF | The PcrA/UvrD helicase functions in multiple pathways that promote bacterial genome stability including the suppression of conflicts between | Find, read and cite all the research you Request PDF | Resolving Holliday Junctions with Escherichia coli UvrD Helicase | The Escherichia coli UvrD helicase is known to function in the mismatch repair and nucleotide excision repair 2006-08-25 UvrD helicase-RNA polymerase interactions are governed by UvrD's carboxy-terminal Tudor domain. Coronavirus: Find the latest articles and preprints Sign in or create an account 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 … The structure and function of an RNA polymerase interaction domain in the PcrA/UvrD helicase: Authors: Sanders, K Lin, C-L Smith, AJ Cronin, N Fisher, G Eftychidis, V McGlynn, P Savery, NJ Wigley, DB Dillingham, MS: Item Type: Journal Article: Abstract: PDF | Nucleotide excision repair (NER) is a general DNA repair mechanism that is capable of removing a wide variety of DNA lesions induced by physical | Find, read and cite all the research you 2009-04-03 · 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 single-stranded DNA. The mismatch repair protein MutL is known to stimulate UvrD.