ArticleNucleic acids research2014
Cellular location and activity of Escherichia coli RecG proteins shed light on the function of its structurally unresolved C-terminus.
Article in Nucleic acids research, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 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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Who cites it
12 citing papers in PubMed.
- The ω subunit stabilizes transcribing RNA polymerase to balance processivity and collision resolution.bioRxiv : the preprint server for biology · 2026Article
- Article
- Replication stalling activates SSB for recruitment of DNA damage tolerance factors.Proceedings of the National Academy of Sciences of the United States of America · 2022Article
- Stimulation of homologous recombination in plants expressing heterologous recombinases.BMC plant biology · 2020Article
- Too Much of a Good Thing: How Ectopic DNA Replication Affects Bacterial Replication Dynamics.Frontiers in microbiology · 2020Review
- Chromosomal over-replication in Escherichia coli recG cells is triggered by replication fork fusion and amplified if replichore symmetry is disturbed.Nucleic acids research · 2018Article
- Dynamics of the Interaction of RecG Protein with Stalled Replication Forks.Biochemistry · 2018Article
- SSB and the RecG DNA helicase: an intimate association to rescue a stalled replication fork.Protein science : a publication of the Protein Society · 2017Review
- Different genome stability proteins underpin primed and naïve adaptation in E. coli CRISPR-Cas immunity.Nucleic acids research · 2015Article
- Article
- I came to a fork in the DNA and there was RecG.Progress in biophysics and molecular biology · 2015Review
- Article
Corrections and comments
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Authors and funding
7 authors.
Funding
Abstract
RecG is a DNA translocase encoded by most species of bacteria. The Escherichia coli protein targets branched DNA substrates and drives the unwinding and rewinding of DNA strands. Its ability to remodel replication forks and to genetically interact with PriA protein have led to the idea that it plays an important role in securing faithful genome duplication. Here we report that RecG co-localises with sites of DNA replication and identify conserved arginine and tryptophan residues near its C-terminus that are needed for this localisation. We establish that the extreme C-terminus, which is not resolved in the crystal structure, is vital for DNA unwinding but not for DNA binding. Substituting an alanine for a highly conserved tyrosine near the very end results in a substantial reduction in the ability to unwind replication fork and Holliday junction structures but has no effect on substrate affinity. Deleting or substituting the terminal alanine causes an even greater reduction in unwinding activity, which is somewhat surprising as this residue is not uniformly present in closely related RecG proteins. More significantly, the extreme C-terminal mutations have little effect on localisation. Mutations that do prevent localisation result in only a slight reduction in the capacity for DNA repair.
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Registered trials
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