tr B5WWL1 B5WWL1_PSEAE Hypothetical membrane protein

tr A9W9N7 A9W9N7_CHLAA Putative uncharacterized protein

Periplasmic. Outer Membrane. Extracellular. Unknown. View in JBrowse View in GBrowse PseudoCyc / Metabolic Pathways.

Uvrd function

All of these proteins function in a network that determines where and how RecA functions. Additional regulatory proteins may remain to be discovered. 2019-08-13 Escherichia coli UvrD is a 3′–5′ superfamily 1A helicase/translocase involved in a variety of DNA metabolic processes. 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.

Replikation – transkriptionskonflikter i bakterier - naturen

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. Our results suggest that UvrD and other NER pathway proteins play a prominent role in maintaining genome integrity, especially after DNA damage; thus, NER may be especially critical in organisms such as H. pylori that face high-level genotoxic stress in vivo.

Replikation – transkriptionskonflikter i bakterier - naturen

Periplasmic. Outer Membrane. Extracellular. Unknown. View in JBrowse View in GBrowse PseudoCyc / Metabolic Pathways.

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 [17]. 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.
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2020-10-23 · This feature of UvrD-CTD points to an essential function as a protein-ligand binding hub facilitating the RNAP interaction.

In bacteria, UvrD-like helicases generally function as components of larger molecular machines , , , , .
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Key Publications University of Gothenburg

UvrD couples ATP binding and hydrolysis to unwind double-stranded DNA and translocate along ssDNA with 3'-to-5' directionality. 2009-02-23 · Expansion occurred at an increased rate in cells lacking dam, polA, rnhA, or uvrD functions. Null mutations of various other cellular recombination, repair, and stress response genes had little effect upon expansion. The red recombination genes of phage lambda could substitute for recBCD in mediating expansion.

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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. 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 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. UvrD, a helicase with multiple functions in vivo, one of which is to remove RecA from ssDNA (Veaute et al.

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InterPro provides functional analysis of proteins by classifying them into families and predicting domains and important sites. We combine protein signatures UvrA and UvrB are precipitated with UvrD in solution ability of UvrD-HIS to function in UvrABC-mediated expressed UvrD-HIS protein retains its function in . helicase for replication bypass protein blocks, a function similar to the Rep and UvrD helicases (33). These helicases can reduce replisome pausing at several In this study, we characterized the role UvrD has in processing and restoring replication forks following arrest by UV-induced DNA damage.

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 . UvrD might therefore function to inhibit formation of recombination intermediates at blocked forks (Magner et al., 2007).Here, we demonstrate that Rep and UvrD promote movement of replisomes along proteinbound DNA regardless of the identity of the blocking nucleoprotein complex, that transcription complexes present the most significant of such blocks in vivo, and that accessory helicase 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 In addition, we succeeded in constructing a uvrD rep double mutant when E. coli cells harboured the pcrA‐encoding plasmid (not shown). The viability of such strains suggests that PcrA provides precisely the function of UvrD that is essential in a rep background, or the function of Rep that is essential in a uvrD … 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 helicase activity.