ArticleThe EMBO journal2003
A model for dsDNA translocation revealed by a structural motif common to RecG and Mfd proteins.
Article in The EMBO journal, 2003. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 52 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
52 citing papers in PubMed, 89 citations in OpenAlex.
- Mechanism of transcription modulation by the transcription-repair coupling factor.Nucleic acids research · 2022Article
- Conserved motifs in the flavivirus NS3 RNA helicase enzyme.Wiley interdisciplinary reviews. RNA · 2022Review
- Single-molecule studies of helicases and translocases in prokaryotic genome-maintenance pathways.DNA repair · 2021Review
- Mfd - at the crossroads of bacterial DNA repair, transcriptional regulation and molecular evolvability.Transcription · 2021Review
- Article
- A Peek Inside the Machines of Bacterial Nucleotide Excision Repair.International journal of molecular sciences · 2021Review
- Structural basis of Mfd-dependent transcription termination.Nucleic acids research · 2020Article
- The mechanism of Single strand binding protein-RecG binding: Implications for SSB interactome function.Protein science : a publication of the Protein Society · 2020Article
- DNA Helicase-SSB Interactions Critical to the Regression and Restart of Stalled DNA Replication forks inGenes · 2020Review
- Nanoscale interaction of RecG with mobile fork DNA.Nanoscale advances · 2020Article
- Movement of the RecG Motor Domain upon DNA Binding Is Required for Efficient Fork Reversal.International journal of molecular sciences · 2018Article
- Dynamics of the Interaction of RecG Protein with Stalled Replication Forks.Biochemistry · 2018Article
- RecG controls DNA amplification at double-strand breaks and arrested replication forks.FEBS letters · 2017Review
- SSB and the RecG DNA helicase: an intimate association to rescue a stalled replication fork.Protein science : a publication of the Protein Society · 2017Review
- Mfd Protein and Transcription-Repair Coupling in Escherichia coli.Photochemistry and photobiology · 2017Review
- Article
- Mycobacterium tuberculosis RecG protein but not RuvAB or RecA protein is efficient at remodeling the stalled replication forks: implications for multiple mechanisms of replication restart in mycobacteria.The Journal of biological chemistry · 2015Article
- The RECG1 DNA Translocase Is a Key Factor in Recombination Surveillance, Repair, and Segregation of the Mitochondrial DNA in Arabidopsis.The Plant cell · 2015Article
- Escherichia coli radD (yejH) gene: a novel function involved in radiation resistance and double-strand break repair.Molecular microbiology · 2015Article
- I came to a fork in the DNA and there was RecG.Progress in biophysics and molecular biology · 2015Review
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
5 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
RecG protein differs from other helicases analysed to atomic resolution in that it mediates strand separation via translocation on double-stranded (ds) rather than single-stranded (ss) DNA. We describe a highly conserved helical hairpin motif in RecG and show it to be important for helicase activity. It places two arginines (R609 and R630) in opposing positions within the component helices where they are stabilized by a network of hydrogen bonds involving a glutamate from helicase motif VI. We suggest that disruption of this feature, triggered by ATP hydrolysis, moves an adjacent loop structure in the dsDNA-binding channel and that a swinging arm motion of this loop drives translocation. Substitutions that reverse the charge at R609 or R630 reduce DNA unwinding and ATPase activities, and increase dsDNA binding, but do not affect branched DNA binding. Sequences forming the helical hairpin and loop structures are highly conserved in Mfd protein, a transcription-coupled DNA repair factor that also translocates on dsDNA. The possibility of type I restriction enzymes and chromatin-remodelling factors using similar structures to drive translocation on dsDNA is discussed.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.