ArticleMolecular microbiology2015
Repair of transposable phage Mu DNA insertions begins only when the E. coli replisome collides with the transpososome.
Article in Molecular microbiology, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
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Who cites it
11 citing papers in PubMed.
- Identification of proteins influencing CRISPR-associated transposases for enhanced genome editing.Science advances · 2026Article
- Ultraconserved bacteriophage genome sequence identified in 1300-year-old human palaeofaeces.Nature communications · 2024Article
- Article
- Targeted transposition with Tn7 elements: safe sites, mobile plasmids, CRISPR/Cas and beyond.Molecular microbiology · 2019Review
- Guidelines for DNA recombination and repair studies: Cellular assays of DNA repair pathways.Microbial cell (Graz, Austria) · 2019Review
- Phage Mu Gam protein promotes NHEJ in concert withProceedings of the National Academy of Sciences of the United States of America · 2018Article
- Article
- Host factors that promote retrotransposon integration are similar in distantly related eukaryotes.PLoS genetics · 2017Article
- Review
- DNA Transposition at Work.Chemical reviews · 2016Review
- Single strand transposition at the host replication fork.Nucleic acids research · 2016Article
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Authors and funding
2 authors.
Funding
Abstract
We report a new cellular interaction between the infecting transposable phage Mu and the host Escherichia coli replication machinery during repair of Mu insertions, which involves filling-in of short target gaps on either side of the insertion, concomitant with degradation of extraneous long flanking DNA (FD) linked to Mu. Using the FD as a marker to follow repair, we find that after transposition into the chromosome, the unrepaired Mu is indefinitely stable until the replication fork arrives at the insertion site, whereupon the FD is rapidly degraded. When the fork runs into a Mu target gap, a double strand end (DSE) will result; we demonstrate fork-dependent DSEs proximal to Mu. These findings suggest that Pol III stalled at the transpososome is exploited for co-ordinated repair of both target gaps flanking Mu without replicating the intervening 37 kb of Mu, disassembling the stable transpososome in the process. This work is relevant to all transposable elements, including retroviral elements like HIV-1, which share with Mu the common problem of repair of their flanking target gaps.
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