ArticleProceedings of the National Academy of Sciences of the United States of America2014
Mu transpososome and RecBCD nuclease collaborate in the repair of simple Mu insertions.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
What it found
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Who cites it
10 citing papers in PubMed, 14 citations in OpenAlex.
- De novo-engineered guide RNA-directed transposition with TnpB-family proteins.Molecular cell · 2026Article
- Identification of proteins influencing CRISPR-associated transposases for enhanced genome editing.Science advances · 2026Article
- Unexplored diversity and ecological functions of transposable phages.The ISME journal · 2023Article
- Targeted transposition with Tn7 elements: safe sites, mobile plasmids, CRISPR/Cas and beyond.Molecular microbiology · 2019Review
- Phage Mu Gam protein promotes NHEJ in concert withProceedings of the National Academy of Sciences of the United States of America · 2018Article
- Article
- Mu-driven transposition of recombinant mini-Mu unit DNA in the Corynebacterium glutamicum chromosome.Applied microbiology and biotechnology · 2018Article
- DNA Transposition at Work.Chemical reviews · 2016Review
- Repair of transposable phage Mu DNA insertions begins only when the E. coli replisome collides with the transpososome.Molecular microbiology · 2015Article
- Controlling DNA degradation from a distance: a new role for the Mu transposition enhancer.Molecular microbiology · 2014Article
Corrections and comments
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
The genome of transposable phage Mu is packaged as a linear segment, flanked by several hundred base pairs of non-Mu DNA. The linear ends are held together and protected from nucleases by the phage N protein. After transposition into the Escherichia coli chromosome, the flanking DNA (FD) is degraded, and the 5-bp gaps left in the target are repaired to generate a simple Mu insertion. Our study provides insights into this repair pathway. The data suggest that the first event in repair is removal of the FD by the RecBCD exonuclease, whose entry past the N-protein block is licensed by the transpososome. In vitro experiments reveal that, when RecBCD is allowed entry into the FD, it degrades this DNA until it arrives at the transpososome, which presents a barrier for further RecBCD movement. RecBCD action is required for stimulating endonucleolytic cleavage within the transpososome-protected DNA, leaving 4-nt flanks outside both Mu ends. This end product of collaboration between the transpososome and RecBCD resembles the intermediate products of Tn7 and retroviral and retrotransposon transposition, and may hint at a common gap-repair mechanism in these diverse transposons.
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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.