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.

2006-08-01

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.

Uvrd helicase function

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. 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. 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).

Reference, Petit MA, Dervyn E, Rose M, Entian KD, McGovern S, Ehrlich SD, Bruand C. PcrA is an essential DNA helicase of Bacillus subtilis fulfilling functions

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. 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).

2018-04-17

UvrD, but not Rep, plays a role of RecA nucleoprotein filament remover in E. coli.

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.
Dela bil

Workflow. Helicases are a class of enzymes vital to all organisms. Their main function is to unpack an organism's genes.

Characterization of this protein indicates that the T. thermophilus UvrD pos-sesses a 3-5 DNA helicase activity similar to the E. coli UvrD … 2018-10-19 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 specificity of isothermal amplification reactions, particularly in conjunction with the WarmStart® LAMP Kit (DNA & … Bacterial UvrD helicase. 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. UvrD helicase activation by MutL involves rotation of its 2B subdomain Yerdos A. Ordabayeva, Binh Nguyena, Alexander G. Kozlova, Haifeng Jiaa, and Timothy M. Lohmana,1 aDepartment of Biochemistry and Molecular Biophysics, Washington University School of Medicine, St. Louis, MO 63110 Edited by Peter H. von Hippel, University of Oregon, Eugene, OR, and approved July 11, 2019 (received for review 2006-08-01 Their main function is to unpack an organism's genes.
Dwg program to open

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.

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 Inactivation of the helicase function of UvrD.

2009-04-03

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. 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 Escherichia coli UvrD DNA helicase functions in several DNA repair processes. 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.