30 Mar 2015 The Escherichia coli UvrD protein is a superfamily 1 (SF1) DNA helicase/ translocase that functions in methyl-directed mismatch repair (MMR) (1,2)

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.

The Rep family helicases are composed of four structural domains. The Rep family function as dimers. REP helicases catalyse ATP dependent unwinding of double stranded DNA to single stranded DNA. 2013-10-15 · This phenotype is further enhanced in cells in which both uvrD and recD2 genes have been disrupted, suggesting that the 5′-3′ helicase, drRecD2, may in part back-up drUvrD’s function. While further studies will be needed to decipher the detailed molecular mechanisms that regulate the helicase activities of dr UvrD, these observations suggest that in vivo both helicase activities of dr Chemla's lab team looked at the structure-function relationship in the helicase UvrD, a protein, found in the bacterium E. coli, that separates strands of DNA in need of repair by unwinding and The structure and function of an RNA polymerase interaction domain in the PcrA/UvrD helicase Kelly Sanders, Chia Liang Lin, Abigail J. Smith , Nora Cronin, Gemma Fisher, Vasileios Eftychidis, Peter McGlynn, Nigel J. Savery , Dale B. Wigley, Mark S. Dillingham * When we have two UvrD molecules, it seems to unwind much further and doesn’t go back and forth as much.” Chemla’s team also resolved one question on the structure-function relationship in UvrD. There are two distinct structures or states that are associated with UvrD, with the molecule organized in either an “open” or “closed” position.

All of these proteins function in a network that determines where and how RecA functions. Additional regulatory proteins may remain to be discovered. 2019-08-13 Escherichia coli UvrD is a 3′–5′ superfamily 1A helicase/translocase involved in a variety of DNA metabolic processes. UvrD can function either as a helicase or only as an single‐stranded DNA (ssDNA) translocase. The switch between these activities is controlled in vitro by the UvrD oligomeric state; a monomer has ssDNA translocase activity, whereas at least a dimer is needed for 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.

2020 — UvrD helicase-RNA polymerase interactions are governed by UvrD's Function, and Can Transdifferentiate into Brown-like Adipocytes. He investigates macromolecular protein machines by high-resolution Nuclear Magnetic Resonance (NMR) underlying essential cellular functions. Group home (strain ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228) GN=uvrD PE=4 function in citronellol catabolism OS=Pseudomonas aeruginosa (strain ATCC UvrD/REP helicase OS=Chloroflexus aurantiacus (strain ATCC 29366 / DSM >tr|A9WAY8|A9WAY8_CHLAA Cell envelope-related function transcriptional 116, CLS10264, n, Y, n, Y, Y, Y, n, 1, 1, 1, 1, 2, 0, 0, 0, 0, 0, UvrD/REP helicase family protein 0, 0, protein of unknown function DUF305 conserved in bacteria.

Amplification and Magnetics) functions by capturing single DNA molecules on Characterization of a thermostable UvrD helicase and its participation in

As a monomer, UvrD can translocate rapidly and processively along ssDNA; however, the monomer is a poor helicase. To unwind duplex DNA in vitro, UvrD needs to be activated either by self-assembly to form a dimer or by interaction with an accessory protein. Interestingly, homologs of UvrD remain present in these species, suggesting that our findings for H. pylori may be applicable to other MMR-deficient organisms as well and that UvrD function, possibly due to its involvement in NER as well as its independent functions, has been retained.

Strongly sensitive to UV, ciprofloxacin (CFX), and azidothymidine (AZT) in single deletion mutants, radA-uvrD double deletions are more sensitive yet. Adding recF mutations almost completely suppresses AZT and partially suppresses UV and CFX sensitivity, suggesting RadA processes a class of intermediates that accumulate in uvrD mutants (PubMed: 25484163 ). 1 Publication

UvrD couples ATP binding and hydrolysis to unwind double-stranded DNA and translocate along ssDNA with 3'-to-5' directionality.

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 also participates in the UvrABC nucleotide excision repair pathway by removing the 12–13-base oligonucleotide containing a pyrimidine dimer or bulky adduct . Additional functions for UvrD have been proposed, consistent with the pleiotropic nature of uvrD mutants (4, 5, 7), including roles in replication and recombination (8–12). Thus, their somewhat different result might reflect altered function or partial activities of the mutant UvrD protein rather than UvrD removal. The data in Figure 1C imply that the increased TLD in strains lacking UvrD results from two separate causes: part from the increased persistence of RecA on DNA when UvrD is absent and part independent of the enhancement of a RecA-dependent TLD pathway. UvrABC endonuclease is a multienzyme complex in bacteria involved in DNA repair by nucleotide excision repair, and it is, therefore, sometimes called an excinuclease. This UvrABC repair process, sometimes called the short-patch process, involves the removal of twelve nucleotides where a genetic mutation has occurred followed by a DNA polymerase, replacing these aberrant nucleotides with the correct nucleotides and completing the DNA repair.
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Function. Helicases are often used to separate strands of a DNA double helix or a self-annealed RNA molecule using the energy from ATP hydrolysis, a process characterized by the breaking of hydrogen bonds between annealed nucleotide bases. They also function to remove nucleic acid-associated proteins and catalyze homologous DNA recombination.

All of these proteins function in a network that determines where and how RecA functions.
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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

The Escherichia coli UvrD protein is a superfamily 1 (SF1) DNA helicase/translocase that functions in methyl-directed mismatch repair (MMR) (1, 2), nucleotide excision repair (NER) and more broadly in genome integrity maintenance.