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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. Conversely, functional assays usually provide little information on structural conformation.

Abstract. 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. Escherichia coli UvrD is a superfamily 1 DNA helicase and single-stranded DNA (ssDNA) translocase that functions in DNA repair and plasmid replication and as an anti-recombinase by removing RecA protein from ssDNA. UvrD couples ATP binding and hydrolysis to unwind double-stranded DNA and translocate along ssDNA with 3'-to-5' directionality.

UvrD, a helicase with multiple functions in vivo, one of which is to remove RecA from ssDNA (Veaute et al. 2005), also promotes TLD resistance in that uvrD null mutants are TLD hypersensitive (Siegal 1973). Understanding how cells become TLD hypersensitive and deﬁning the pathways and mechanisms of action of the proteins that allow cells to resist 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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Adding recF mutations almost completely suppresses AZT and partially suppresses UV and CFX sensitivity, suggesting RadA processes a class of intermediates that accumulate in uvrD mutants (PubMed: 25484163 ). 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 ].

Nucleic Acid Based Pathogen Diagnostics Michael S. Akhras

We previously reported that to remove DNA‐bound Tus protein, UvrD acts in concert with RecBCD‐dependent homologous recombination (Bidnenko et al, 2006). Since UvrD proteins are thought to usually function as dimers , the apparent dominance of the mutant allele could result from forming nonfunctional heteromultimers. 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.
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The Rep family helicases are composed of four structural domains.

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. Initiates unwinding more efficiently from a nicked substrate than ds duplex DNA (PubMed: 8419285 ).
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tr B5WWL1 B5WWL1_PSEAE Hypothetical membrane protein

The UvrD helicase removes RecA filaments from RecA. 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.

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Facilitation by UvrAB of nicked duplex unwinding by UvrD provides an explanation as to why UvrA, -B, and -D are all required to maintain viability in the absence of DNA polymerase I ( 51 ). measurements simultaneously. Here we present measurements of UvrD, a DNA repair helicase, that directly and unambiguously reveal the connection between its structure and function. Our data reveal that UvrD exhibits two distinct types of unwinding activity regulated by its stoichiometry.

Nucleic Acid Based Pathogen Diagnostics Michael S. Akhras

Furthermore, two UvrD conformational states, termed 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 This video provides two examples of how to determine function values using function notation on the TI84 graphing calculator. The results are verified graph Using a combination of both ethyl methanesulfonate and site-directed mutagenesis, we have identified a region in DNA helicase II (UvrD) from Escherichia coli that is required for biological function but lies outside of any of the seven conserved motifs (T. C. Hodgman, Nature 333:22–23, 1988) associated with the superfamily of proteins of which it is a member. Abstract. 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.

Extracellular. Unknown. View in JBrowse View in GBrowse PseudoCyc / Metabolic Pathways. Overview. 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 ].