Key Publications University of Gothenburg

Gelica Se – Resep Kuini

Therefore, helicase assays were carried out using fixed concentration (40 n m ) of HiUvrD or HpUvrD and different DNA structures (Table S2, structures 1–9; 1 n m each), which were used in the DNA‐binding studies. 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 2010-07-09 2012-03-09 2017-02-04 2020-10-23 1988-04-01 UvrD is a DNA helicase that participates in nucleotide excision repair and several replication-associated processes, including methyl-directed mismatch repair and recombination. UvrD is capable of displacing oligonucleotides from synthetic forked DNA structures in vitro and is essential for viability in the absence of Rep, a helicase associated with processing replication forks. 2019-08-13 UvrD (DNA helicase II) has been implicated in DNA replication, DNA recombination, nucleotide excision repair, and methyl-directed mismatch repair.

Uvrd helicase function

Workflow. Helicases are a class of enzymes vital to all organisms. Their main function is to unpack an organism's genes. They are motor proteins that move directionally along a nucleic acid phosphodiester backbone, separating two annealed nucleic acid strands such as DNA and RNA (hence helic- + -ase), using energy from ATP hydrolysis. 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. 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. 2020-10-23 · 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 Bacterial UvrD helicase.

Key Publications University of Gothenburg

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.

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As a monomer, UvrD can translocate rapidly and proc-essively 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 acces-sory protein. 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. 2003-01-31 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 For the XPD helicase in eukaryotic NER a similar function in analogy to UvrB has been proposed, whereas XPB the second helicase uses only its ATPase activity during eukaryotic NER. In prokaryotic mismatch repair (MMR) UvrD again plays a central role.

#=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.
Julfilmer 2021

UvrD is capable of displacing oligonucleotides from synthetic forked DNA structures in vitro and is essential for viability in the absence of Rep, a helicase associated with processing replication forks. 2019-08-13 UvrD (DNA helicase II) has been implicated in DNA replication, DNA recombination, nucleotide excision repair, and methyl-directed mismatch repair.

Helicases are a class of enzymes vital to all organisms. Their main function is to unpack an organism's genes.
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Replikation – transkriptionskonflikter i bakterier - naturen

2003-01-31 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 For the XPD helicase in eukaryotic NER a similar function in analogy to UvrB has been proposed, whereas XPB the second helicase uses only its ATPase activity during eukaryotic NER. In prokaryotic mismatch repair (MMR) UvrD again plays a central role. 2010-07-09 1997-01-17 2009-04-03 2015-04-17 However, there have been conflicting reports about the oligomeric state of the active helicase in vitro, some claiming that a UvrD monomer can function as a processive helicase 36,37, whereas 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. John Atkinson, Colin P. Guy, Chris J. Cadman, Geri F. Moolenaar, Nora Goosen, Peter McGlynn #=GF ID UvrD-helicase #=GF AC PF00580.22 #=GF DE UvrD/REP helicase N-terminal domain #=GF AU Bateman A;0000-0002-6982-4660 #=GF SE MRC-LMB Genome group.

tr B3KYW5 B3KYW5_PLAKH SICA antigen Fragment OS

In addition, UvrD interacts with many other UvrD is a DNA helicase that participates in nucleotide excision repair and several replication-associated processes, including methyl-directed mismatch repair and recombination. UvrD is capable of displacing oligonucleotides from synthetic forked DNA structures in vitro and is essential for viability in the absence of Rep, a helicase associated with processing replication forks.

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.