Kurland, Charles G.; Andersson, Siv G. E.; Zomorodipour, Alireza

Björn Marcus Burmann Göteborgs universitet

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. Function.

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. 2011-09-01 2015-04-17 2014-01-08 2017-02-04 In addition, UvrD plays critical roles in rolling circle plasmid replication, processing of Okazaki fragments in the absence of DNA polymerase I and replication fork reversal in Escherichia coli polymerase III mutants with multiple functions at inactivated replication forks [[8-11]]. The UvrD helicase removes RecA filaments from RecA. All of these proteins function in a network that determines where and how RecA functions.

Nucleic Acid Based Pathogen Diagnostics Michael S. Akhras

2012-03-09 · UvrD functions as a dimer and differs from DnaB mechanistically in that it binds directly to the junction to unwind the DNA leading to a double-stranded product. UvrD does not require a ssDNA tail to initiate the unwinding reaction. RecG unwinds HJs by binding to the crossover site and unwinding to produce a two-strand product .

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2012-05-09 · 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. 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. We find that H. pylori UvrD functions to repair DNA damage and limit homologous recombination and DNA damage-induced genomic rearrangements between DNA repeats.

Eftersom dessa fyra gener är närvarande över alla 53 stammar, undersökte vi deras integritet. För var UvrD-like DNA helicase, C-terminal 279 618 1.4E-75 CDD cd18807 SF1_C_UvrD 287 616 5.00011E-31 ProSiteProfiles PS51198 UvrD-like DNA helicase ATP-binding domain profile. IPR014016: UvrD-like helicase, ATP-binding domain 10 288 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. Initiates unwinding more efficiently from a nicked substrate than ds duplex DNA (PubMed: 8419285 ). Involved in the post-incision events of nucleotide excision repair and methyl-directed mismatch repair, and probably also in repair of alkylated DNA (Probable).1 Publication. 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. The reported ability of PcrA/UvrD to bind and backtrack RNA polymerase (1,2) might be relevant to these functions, but the structural basis for this activity is poorly understood. Function DNA Damage Recognition by UvrA.
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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.

Such regulation is likely important in vivo since an unregulated helicase would likely be detrimental to the cell. In bacteria, UvrD-like helicases generally function as components of larger molecular machines , , , , . 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. 2009-04-03 · Whether this protein displacement function requires specific recruitment of UvrD or merely reflects the abundance of UvrD in vivo remains unknown.
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Key Publications University of Gothenburg

We developed a single-molecule technique combining optical tweezers and fluorescence microscopy that allows for both measurements simultaneously. Here we present measurements of UvrD, a DNA repair 2018-10-19 2009-04-03 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). Nucleic Acids Research, 2017 1 doi: 10.1093/nar/gkx074 The structure and function of an RNA polymerase interaction domain in the PcrA/UvrD helicase Kelly Sanders1,†, Chia-Liang Lin2,†, Abigail J. Smith1,†, Nora Cronin2, Gemma Fisher1, Vasileios Eftychidis3, Peter McGlynn3, Nigel J. Savery1, Dale B. Wigley2 and Mark S. Dillingham1,* 1DNA:Protein Interactions Unit, School of Biochemistry 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 thermophilic organism Thermoanaerobacter tengcongensis.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 This video provides two examples of how to determine function values using function notation on the TI84 graphing calculator. The results are verified graph Rep and UvrD helicases displayed a similar behavior, we ﬁrst examined ATPase activity in the presence of each fork substrate as a function of magnesium ion concentration.