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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. Under these conditions, Rep displayed optimal activity at 0.5 mM magnesium ion, whereas UvrD exhibited optimal activity at 1 mM (Figure 1A,B). There was one exception to 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.
Outer Membrane. Extracellular. Unknown. View in JBrowse View in GBrowse PseudoCyc / Metabolic Pathways. Overview.
The specific role of these mutations in 44 (mutH, mutL, mutS, uvrD) indikerar en mutatorspänning. Eftersom dessa fyra gener är närvarande över alla 53 stammar, undersökte vi deras integritet.
tr A9W9N7 A9W9N7_CHLAA Putative uncharacterized protein
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.
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The requirements for using UvrB binding to DNA were examined by UvrB and UvrC Interaction.
UvrD couples ATP binding and hydrolysis to unwind double-stranded DNA and translocate along ssDNA with 3'-to-5' directionality. 2009-02-23
UvrD function on these substrates. For substrate 3, omission of. SSB resulted in increased unwinding by UvrD in the absence of. UvrAB (compare Fig. 4, A (lane 5) and B, with Fig. 5 A (lane 6)
uvrD in E. coli remains viable, although it is lethal in either a polA or rep background, and exhibits sensiti-vity to UV light, elevated rates of recombination and mutations . This multitude of functions of UvrD make it important to all organisms, more so in patho-genic bacteria or extremophiles surviving under
In contrast, suppression by altered patterns of gene expression or by bypass of Rep/UvrD function in transcription would not entail any reduced ability of replisomes to move along protein-bound DNA. We tested, therefore, whether Δ rep Δ uvrD rpoB∗35 cells had a reduced ability to tolerate nucleoprotein complexes as compared with rep+ uvrD+ rpoB∗35 cells or cells lacking only one helicase. 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.There are many helicases, representing the great variety of processes in
They quantitively characterized the self-assembly equilibria of wild-type UvrD as a function of NaCl and glycerol concentrations as well astemperature using analytical ultracentrifugation and concluded that a lower NaCl concentration, a lower pH, a lower glycerol concentration, and a higher temperature were favorable for UvrD oligomer formation .
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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 & RNA). Workflow UvrD (DNA helicase II) is a prototypical superfamily 1 (SF 1) helicase involved primarily in nucleotide excision repair and methyl-directed mismatch repair in Escherichia coli (1, 2).
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tr B5WWL1 B5WWL1_PSEAE Hypothetical membrane protein
1 Publication During replication, UvrD function is required to displace the nascent DNA strand during methyl-directed mismatch repair, a replication-coupled process that removes mispaired bases [20, 21]. It is required for replication of several rolling-circle plasmids [ 22 ] and copurifies with DNA polymerase III holoenzyme under some conditions [ 23 ].
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Kurland, Charles G.; Andersson, Siv G. E.; Zomorodipour, Alireza
Cytoplasmic Membrane. Periplasmic. Outer Membrane. Extracellular. Unknown.
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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. 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. 1998-01-15 2015-03-30 and function must be inferred.
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.