UvrD helicase, unlike Rep helicase, dismantles RecA nucleoprotein filaments in Escherichia coli

Veaute, Xavier; Delmas, Stéphane; Selva, M. La; Jeusset, Josette; Cam, Eric Le; Matić, Ivan; Fabre, Francis; Petit, Marie‐Agnès

doi:10.1038/sj.emboj.7600485

Cited by 242 publications

(282 citation statements)

References 69 publications

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“…Current models suggest that UvrD removes RecA assembled on single-stranded DNA (ssDNA) at a blocked replication fork to allow replication fork reversal to occur (15). This is consistent with in vitro experiments that have shown UvrD to be capable of removing RecA molecules from DNA thereby disrupting a recombination event (9,18,18,19). It has also been suggested that UvrD could act to resolve the intermediate formed by replication fork regression so that the lesion may be repaired or bypassed immediately (16,20).…”

supporting

confidence: 61%

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Resolving Holliday Junctions with Escherichia coli UvrD Helicase

Tahmaseb

Compton

et al. 2012

Journal of Biological Chemistry

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supporting

confidence: 61%

“…In addition, UvrD has been shown to unwind RNA-DNA hybrids (41) as well as displacing RecA bound to ssDNA (9,19). The promiscuous unwinding activity of UvrD is likely a reflection of its multiple roles in the cell including roles in repair, replication, and recombination consistent with the pleiotropic phenotype of uvrD mutants (1).…”

Section: Discussionmentioning

confidence: 93%

Resolving Holliday Junctions with Escherichia coli UvrD Helicase

Tahmaseb

Compton

et al. 2012

Journal of Biological Chemistry

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“…Pre-initiation complexes spontaneously isomerize under these conditions to yield an open complex, with the two DNA strands separated from approximately Ϫ3 to ϩ8, relative to the site of initiation (ϩ1), to form a transcription bubble. 6 The ability of the MCM helicase to unwind this DNA when bound into pre-initiation complexes (Fig. 4) was determined when the directions of helicase movement and transcription were the same (co-direction; Fig.…”

Section: Resultsmentioning

confidence: 99%

Archaeal Minichromosome Maintenance (MCM) Helicase Can Unwind DNA Bound by Archaeal Histones and Transcription Factors

Shin

Santangelo

Xie

et al. 2007

Journal of Biological Chemistry

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Protein-DNA complexes must be disassembled to facilitate DNA replication. Replication forks contain a helicase that unwinds the duplex DNA at the front of the fork. The minichromosome maintenance helicase from the archaeon Methanothermobacter thermautotrophicus required only ATP to unwind DNA bound into complexes by the M. thermautotrophicus archaeal histone HMtA2, transcription repressor TrpY, or into a transcription pre-initiation complex by M. thermautotrophicus TATA-box-binding protein, transcription factor B, and RNA polymerase. In contrast, the minichromosome maintenance helicase was unable to unwind DNA bound by this archaeal RNA polymerase in a stalled transcript-elongating complex.DNA is bound in vivo into complexes by many different proteins, most of which presumably must be displaced to facilitate DNA replication. As DNA helicases are located at the front of the replication machinery, they seem likely to participate in displacing such proteins from DNA, and consistent with this, a number of helicases have been shown to be capable of displacing proteins from DNA. Both Escherichia coli DNA helicase I and Rep protein have the ability to disassociate the LacI repressor from lacO DNA (1), and DnaB can remove Epstein-Barr virus nuclear protein 1 from its binding site on DNA (2). The yeast Pif1 helicase can displace telomerase from telomeric DNA (3), and the yeast Srs2 and bacterial UvrD helicases have been shown to displace Rad51 and RecA, respectively, from singlestranded DNA (ssDNA) 4 (4 -6). E. coli RecBCD and simian virus 40 large T-antigen helicases have been shown to unwind histone-bound DNA (7). However, in vivo, histone acetylation also aids eukaryotic replication fork progress by destabilizing chromatin and eukaryotic histone-DNA interactions (8). Consistent with the coordination of chromatin destabilization and eukaryotic DNA replication, a human replicative helicase minichromosome maintenance (MCM) protein has been shown to interact with both histones (9) and a histone acetyl transferase (10). The machineries responsible for DNA replication and transcription in Archaea have fewer components than their eukaryotic counterparts, but the proteins that are present are closely related in sequence and structure to eukaryotic proteins (11, 12). The reduced complexity of the archaeal systems makes them attractive for experimental investigation, both as inherently interesting systems in their own right and as simpler models directly relevant to understanding eukaryotic DNA replication and transcription. With this in mind, we have established robust in vitro DNA-and RNA-synthesizing systems using purified archaeal components that originate from Methanothermobacter thermautotrophicus and have begun to investigate their regulation (13-15).M. thermautotrophicus has a single MCM helicase that is thought to function as the replicative helicase. Biochemical studies have established that this enzyme has ATP-dependent 3Ј 3 5Ј helicase activity and DNA-dependent ATPase activity, that it can bind and translocate alon...

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“…In temperature-sensitive dnaN and dnaE cells, UvrD has been implicated in the removal of RecA molecules that are bound to the arrested replication forks (13). Similarly, UvrD disrupts RecA bound to synthetic recombination intermediates, and it is hypothesized that in the absence of UvrD, the inability to disrupt RecA filaments leads to the hyper-recombinogenic phenotype (14). In agreement with these conclusions, cells expressing the hyper-helicase mutant of UvrD (UvrD303) have anti-recombinogenic and anti-mutator phenotypes (15,16).…”

mentioning

confidence: 99%

Modulation of UvrD Helicase Activity by Covalent DNA-Protein Cross-links

Kumari

Minko

Smith

et al. 2010

Journal of Biological Chemistry

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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. 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. Although UvrD interactions with proteins bound to DNA have significant biological implications, the effects of covalent DNAprotein cross-links on UvrD helicase activity have not been characterized. Herein, we demonstrate that UvrD-catalyzed strand separation was inhibited on a DNA strand to which a 16-kDa protein was covalently bound. Our sequestration studies suggest that the inhibition of UvrD activity is most likely due to a translocation block and not helicase sequestration on the crosslink-containing DNA substrate. In contrast, no inhibition of UvrD-catalyzed strand separation was apparent when the protein was linked to the complementary strand. The latter result is surprising given the earlier observations that the DNA in this covalent complex is severely bent (ϳ70°), with both DNA strands making multiple contacts with the cross-linked protein. In addition, UvrD was shown to be required for replication of plasmid DNAs containing covalent DNA-protein complexes. Combined, these data suggest a critical role for UvrD in the processing of DNA-protein cross-links.

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UvrD helicase, unlike Rep helicase, dismantles RecA nucleoprotein filaments in Escherichia coli

Cited by 242 publications

References 69 publications

Resolving Holliday Junctions with Escherichia coli UvrD Helicase

Resolving Holliday Junctions with Escherichia coli UvrD Helicase

Archaeal Minichromosome Maintenance (MCM) Helicase Can Unwind DNA Bound by Archaeal Histones and Transcription Factors

Modulation of UvrD Helicase Activity by Covalent DNA-Protein Cross-links

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