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.

16 Feb 2014 UvrD, also known as DNA helicase II is an ATP dependent ssDNA translocase and dsDNA helicase which functions in methyl-directed

Periplasmic. Outer Membrane. Extracellular. Unknown. View in JBrowse View in GBrowse PseudoCyc / Metabolic Pathways. Overview.

Abstract. 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. 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. 2009-02-23 · Expansion occurred at an increased rate in cells lacking dam, polA, rnhA, or uvrD functions.

uvrD in E. coli remains viable, although it is lethal in either a polA or rep background, and exhibits sensiti-vity to UV light, elevated rates of recombination and mutations [17].

We find that H. pylori UvrD functions to repair DNA damage and limit homologous recombination and DNA damage-induced genomic rearrangements between DNA repeats. Our results suggest that UvrD and other NER pathway proteins play a prominent role in maintaining genome integrity, especially after DNA damage; thus, NER may be especially critical in organisms such as H. pylori that face high-level genotoxic stress in vivo.

In conclusion, our results show that UvrD has multiple functions at inactivated replication forks, which are all linked to the action of recombination proteins but by different means. We previously reported that to remove DNA‐bound Tus protein, UvrD acts in concert with RecBCD‐dependent homologous recombination (Bidnenko et al, 2006). Since UvrD proteins are thought to usually function as dimers , the apparent dominance of the mutant allele could result from forming nonfunctional heteromultimers. UvrD, a highly conserved helicase involved in mismatch repair, nucleotide excision repair (NER), and recombinational repair, plays a critical role in maintaining genomic stability and facilitating DNA lesion repair in many prokaryotic species.

2009-04-03

Our results suggest that UvrD and other NER pathway proteins play a prominent role in maintaining genome integrity, especially after DNA damage; thus, NER may be especially critical in organisms such as H. pylori that face high-level … Therefore, the function of UvrD that allows RFR at dnaNts ‐blocked forks in the presence of RecQJFORA is inactivated by the uvrD252 mutation, suggesting a requirement for the helicase or the translocase function of UvrD to counteract RecQJFORA in this replication mutant. The RFR defect of the uvrD mutant is suppressed by Bacillus subtilis PcrA UvrD, a helicase with multiple functions in vivo, one of which is to remove RecA from ssDNA (Veaute et al. 2005), also promotes TLD resistance in that uvrD null mutants are TLD hypersensitive (Siegal 1973). Understanding how cells become TLD hypersensitive and deﬁning the pathways and mechanisms of action of the proteins that allow cells to resist 2012-01-20 RecJ functions in both the RecQ and RecA-dependent TLD pathways in UvrD + cells Whereas, RecA, RecF, RecQ, and RecJ act in one linear pathway of hyper-TLD in Δ uvrD cells ( Figures 3B and Figure 4, A, C, and D ), RecQ and RecJ were shown previously to act in one pathway of TLD in UvrD + cells while RecA and RecF acted in a second SOS-response-dependent pathway that is independent of RecQ ( Fonville et al. … 2020-10-23 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 proteins involved in the above processes and is hypothesized to facilitate protein turnover, thus promoting further DNA processing.

There was one exception to In fact genetically, UvrD functions as an anti-recombinase rather than a recombinase.The need for UvrD in Pol IIIts mutants only when RecQ, RecJ, RecFOR, and RecA are all present led Lestini and Michel (34) to propose that UvrD antagonizes deleterious actions of RecQ-, RecJ-, and RecFOR-dependent RecA binding to arrested forks, which prevents replication fork reversal (RFR) ( Figure 1F,G of 2018-04-17 2017-11-14 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. 2009-02-23 UvrD function on these substrates.
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It is required for replication of several rolling-circle plasmids [ 22 ] and copurifies with DNA polymerase III holoenzyme under some conditions [ 23 ]. RecJ functions in both the RecQ and RecA-dependent TLD pathways in UvrD + cells Whereas, RecA, RecF, RecQ, and RecJ act in one linear pathway of hyper-TLD in Δ uvrD cells ( Figures 3B and Figure 4, A, C, and D ), RecQ and RecJ were shown previously to act in one pathway of TLD in UvrD + cells while RecA and RecF acted in a second SOS-response-dependent pathway that is independent of RecQ ( Fonville et al.

In addition, UvrD interacts with many other proteins involved in the above processes and is hypothesized to facilitate protein turnover, thus promoting further DNA processing. 1998-01-15 2015-03-30 and function must be inferred. Conversely, functional assays usually provide little information on structural conformation. We developed a single-molecule technique combining optical tweezers and fluorescence microscopy that allows for both measurements simultaneously.
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UvrD, a helicase with multiple functions in vivo, one of which is to remove RecA from ssDNA (Veaute et al. 2005), also promotes TLD resistance in that uvrD null mutants are TLD hypersensitive (Siegal 1973). Understanding how cells become TLD hypersensitive and deﬁning the pathways and mechanisms of action of the proteins that allow cells to resist

In contrast, at forks affected for the Pol IIIh clamp (DnaN), RarA is not required for RecA binding and the ATPase function of UvrD is essential to counteract RecA, supporting the idea that UvrD removes RecA from DNA. UvrD action on RecA is conserved in evolution as it can be performed in E. coli by the UvrD homologue from Bacillus subtilis, PcrA. 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. 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 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 proteins involved in the above processes and is hypothesized to facilitate protein turnover, thus promoting further DNA processing. UvrD, a helicase with multiple functions in vivo, one of which is to remove RecA from ssDNA (Veaute et al. 2005), also promotes TLD resistance in that uvrD null mutants are TLD hypersensitive (Siegal 1973). Understanding how cells become TLD hypersensitive and deﬁning the pathways and mechanisms of action of the proteins that allow cells to resist 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.