22 Feb 2021 Accessory replicative helicases in Escherichia coli, Rep and UvrD, help replication machinery overcome blocks by removing incoming

P >tr|A9W9P7|A9W9P7_CHLAA UvrD/REP helicase OS=Chloroflexus aurantiacus (strain ATCC 29366 / DSM 635 / J-10-fl) GN=Caur_1305 PE=4 SV=1

Background: The ability of UvrD, a DNA helicase, to unwind a Holliday junction has not been directly tested. Results: UvrD catalyzed robust unwinding of a Holliday junction producing a forked structure. Conclusion: UvrD unwinds a Holliday junction by binding to the junction and translocating along opposite arms. 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. Product Class: Other Tte UvrD Helicase Need assistance designing LAMP primers? Use the NEB LAMP Primer Design Tool. Product Introduction Unwinds double-stranded DNA Thermostable to 65°C Reduces non-specific product UvrD monomers translocate in discrete steps with an average kinetic step-size, m=3.68 nt step(-1), a translocation rate constant, kt=51.3 steps s(-1), with a processivity corresponding to an average translocation distance of 2400 nt before dissociation PMID: 15561144; mutational analysis of a thermostable UvrD helicase PMID: 15955821 UniProtKB.

Uvrd helicase

These structures reveal that ATP binding alone leads to unwinding of 1 base pair by directional rotation and translation of the DNA duplex, and ADP and Pi release leads to translocation of the developing single strand. The Rep helicase is needed during bacteriophages M13 and ΦX174 replication (Takahashi et al, 1979), the UvrD helicase ensures the replication of Gram‐negative rolling‐circle plasmids (Bruand and Ehrlich, 2000) and the PcrA helicase ensures the replication of Gram‐positive rolling‐circle plasmids (Petit et al, 1998; Anand et al, 2004). Characterization of a Thermostable UvrD Helicase and Its Participation in Helicase-dependent Amplification* Helicase-dependent amplification (HDA) is an isothermal in vitro DNA amplification method based upon the coordinated actions of helicases to separate double-stranded DNA and DNA polymerases to synthesize DNA. UvrD helicase plays essential roles in multiple DNA metabolic processes, including methyl-directed mismatch repair. UvrD monomers can translocate along single-stranded DNA, but self-assembly or interaction with an accessory factor is required to activate processive DNA unwinding in vitro. The most known SF1A helicases are Rep and UvrD in gram-negative bacteria and PcrA helicase from gram-positive bacteria. The most known Helicases in the SF1B group are RecD and Dda helicases.

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In the presence of 10 ng Tte UvrD Helicase (right), the positive reaction maintains its rapid amplification time with a slight reduction in total RFU, while the NTC reaction is completely suppressed. This ability of UvrD to remodel RNAP-DNA complexes might also be relevant to the ability of PcrA/UvrD to suppress conflicts between replication and transcription, a property it shares with the very closely related helicase Rep (although Rep does not interact with RNAP) (26– 28).

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00:00/00:00 UvrD Helicase 01:04:40. 00:00/00:00.

CAS Article Google Scholar 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 2008-03-15 · The well studied E. coli UvrD helicase (helicase II) unwinds DNA in the 3' to 5' direction. Unlike many other helicases, the UvrD helicase is capable of melting fully duplex molecules (DNA fragment with blunt ends) as well as nicked circular DNA molecules. 2006-12-29 · UvrD, originally known as DNA helicase II in E. coli (Hickson et al., 1983), is the founding member of SF1 and unwinds DNA in the 3′→ 5′ direction (Matson and George, 1987). The kinetic mechanism by which the DNA repair helicase UvrD of Escherichia coli unwinds duplex DNA was examined with the use of a series of oligodeoxynucleotides with duplex regions ranging from 10 to 40 base pairs. Single-turnover unwinding experiments showed distinct lag phases that increased with duplex length because partially unwound DNA intermediate states are highly populated during UvrD exhibits modest processivity as a DNA helicase (40–50 bp) (53– 55) making this protein an interesting choice for the helicase responsible for the unwinding event in MMR. UvrD is also the helicase responsible for the unwinding event associated with excision repair ( 56 – 59 ), which requires unwinding of a short 12–13 base long oligonucleotide well within the limits of the processivity of UvrD.
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Abstract. Escherichia coli UvrD is a superfamily 1 helicase/translocase involved 22 Feb 2021 Accessory replicative helicases in Escherichia coli, Rep and UvrD, help replication machinery overcome blocks by removing incoming The roles of UvrD and Rep DNA helicases of Escherichia coli are not yet fully understood. In particular, the reason for rep uvrD double mutant lethality remains the Escherichia coli UvrD helicase, DNA polymerase I. Klenow fragment, two accessory proteins, MutL and sin- gle-stranded DNA-binding protein (SSB), was UvrD helicase unwinds DNA one base pair at a time by a two-part power stroke. Earlier crystal structures have suggested that DNA helicases translocate ABSTRACT.

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UvrD helicase plays essential roles in multiple DNA metabolic processes, including methyl-directed mismatch repair. UvrD monomers can translocate along single-stranded DNA, but self-assembly or interaction with an accessory factor is required to activate processive DNA unwinding in vitro.

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. Structures of UvrD-like SF1 helicase solved so far share a four-subdomain tertiary arrangement (1A/2A/1B/2B) (Singleton et al., 2007), including two RecA-like domains (1A/2A) which contain the ATP binding site and are proposed to function as the translocase (Dillingham et al., 2001; Lee and Yang, 2006), and a flexible domain (2B) which is believed to play a regulatory role in helicase activity Full-length PfUvrD helicase (PFE0705c) along with the location of UvrD domain distributed over the helicase. It is a 1441 amino acid long protein with a conserved UvrD domain from 36 – 801 amino Without Tte UvrD Helicase (left), the positive reaction (+DNA) amplifies in ~8 minutes while the no-template control (NTC) amplifies in ~20 minutes. In the presence of 10 ng Tte UvrD Helicase (right), the positive reaction maintains its rapid amplification time with a slight reduction in total RFU, while the NTC reaction is completely suppressed.

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UvrD exhibits modest processivity as a DNA helicase (40–50 bp) (53– 55) making this protein an interesting choice for the helicase responsible for the unwinding event in MMR. UvrD is also the helicase responsible for the unwinding event associated with excision repair ( 56 – 59 ), which requires unwinding of a short 12–13 base long oligonucleotide well within the limits of the processivity of UvrD.

The role of Rep The P. falciparum genome is available from the Plasmodium helicase has been elucidated in MMR. The progression of repli Direct imaging of single UvrD helicase dynamics on long single-stranded DNA. Nature Communications, 2013. Hamza Balci. Taekjip Ha. Kyung Lee. Haifeng Jia. Timothy Lohman. Jae-hyuk Lee. UvrD monomers translocate in discrete steps with an average kinetic step-size, m=3.68 nt step(-1), a translocation rate constant, kt=51.3 steps s(-1), with a processivity corresponding to an average translocation distance of 2400 nt before dissociation PMID: 15561144; mutational analysis of a thermostable UvrD helicase PMID: 15955821 Full-length PfUvrD helicase (PFE0705c) along with the location of UvrD domain distributed over the helicase. It is a 1441 amino acid long protein with a conserved UvrD domain from 36 – 801 amino UVRD_HELICASE_CTER, PS51217; UvrD-like DNA helicase C-terminal domain profile (MATRIX) Sequences in UniProtKB/Swiss-Prot known to belong to this class: 257. detected by PS51217: 255 (true positives) undetected by PS51217: 2 (2 false negatives and 0 'partial') Other sequence(s) in UniProtKB/Swiss-Prot detected by PS51217: NONE.

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Protocol Protocol for unwinding double stranded DNA with Tte 2017-02-04 UvrD, a ubiquitous bacterial helicase that plays important roles in multiple DNA metabolic pathways, is essential for genome stability and might, therefore, be crucial in bacterial physiology and pathogenesis. In this study, the func-tional characterization of UvrD helicase from Haemophilus inﬂuenzae and Helicobacter pylori is reported.

1988-04-01 · CPX-5542, MutL-UvrD DNA helicase complex: DIP i: DIP-11103N: IntAct i: P03018, 39 interactors: STRING i: 511145.b3813 We report here a series of crystal structures of the UvrD helicase complexed with DNA and ATP hydrolysis intermediates. These structures reveal that ATP binding alone leads to unwinding of 1 base pair by directional rotation and translation of the DNA duplex, and ADP and Pi release leads to translocation of the developing single strand. UvrD had already been found to remove proteins from DNA, but always in a situation coupled with DNA unwinding: in the context of UvrABC‐dependent UV repair, after the incision step mediated by UvrABC, the UvrD helicase was found to remove both the 12‐mer containing the lesion and the UvrC protein (Orren et al, 1992). UvrD helicase plays essential roles in multiple DNA metabolic processes, including methyl-directed mismatch repair. UvrD monomers can translocate along single-stranded DNA, but self-assembly or interaction with an accessory factor is required to activate processive DNA unwinding in vitro. UvrD is a helicase that is widely conserved in gram-negative bacteria. A uvrD homologue was identified in Mycobacterium tuberculosis on the basis of the homology of its encoded protein with Escherichia coli UvrD, with which it shares 39% amino acid identity, distributed throughout the protein.