ArticleProceedings of the National Academy of Sciences of the United States of America2013
Direct interaction between the TnsA and TnsB subunits controls the heteromeric Tn7 transposase.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.
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Who cites it
17 citing papers in PubMed.
- Transposon end recognition and pairing by I-F3 CRISPR-associated transposase.Science advances · 2026Article
- Insights on the regulation and function of the CRISPR/Cas transposition system located in the pathogenicity island VpaI-7 fromInfection and immunity · 2025Article
- Article
- Novel mechanisms of diversity generation in Acinetobacter baumannii resistance islands driven by Tn7-like elements.Nucleic acids research · 2024Article
- Transposons and CRISPR: Rewiring Gene Editing.Biochemistry · 2023Article
- Insight into the molecular mechanism of the transposon-encoded type I-F CRISPR-Cas system.Journal, genetic engineering & biotechnology · 2023Review
- Functional characterization of diverse type I-F CRISPR-associated transposons.Nucleic acids research · 2022Article
- Structure of the TnsB transposase-DNA complex of type V-K CRISPR-associated transposon.Nature communications · 2022Article
- Mechanistic details of CRISPR-associated transposon recruitment and integration revealed by cryo-EM.Proceedings of the National Academy of Sciences of the United States of America · 2022Article
- Structural basis of transposon end recognition explains central features of Tn7 transposition systems.Molecular cell · 2022Article
- Metagenomic discovery of CRISPR-associated transposons.Proceedings of the National Academy of Sciences of the United States of America · 2021Article
- Detection of TnFrontiers in microbiology · 2020Article
- Targeted transposition with Tn7 elements: safe sites, mobile plasmids, CRISPR/Cas and beyond.Molecular microbiology · 2019Review
- Recruitment of CRISPR-Cas systems by Tn7-like transposons.Proceedings of the National Academy of Sciences of the United States of America · 2017Article
- Article
- Mechanisms of DNA Transposition.Microbiology spectrum · 2015Review
- The Tn7 transposition regulator TnsC interacts with the transposase subunit TnsB and target selector TnsD.Proceedings of the National Academy of Sciences of the United States of America · 2014Article
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Authors and funding
4 authors.
Funding
Abstract
The transposon Tn7 transposase that recognizes the transposon ends and mediates breakage and joining is heteromeric. It contains the Tn7-encoded proteins TnsB, which binds specifically to the transposon ends and carries out breakage and joining at the 3' ends, and TnsA, which carries out breakage at the 5' ends of Tn7. TnsA apparently does not bind specifically to DNA, and we have hypothesized that it is recruited to the ends by interaction with TnsB. In this work, we show that TnsA and TnsB interact directly and identify several TnsA and TnsB amino acids involved in this interaction. We also show that TnsA can stimulate two key activities of TnsB, specific binding to the ends and pairing of the Tn7 ends. The ends of Tn7 are structurally asymmetric (i.e., contain different numbers of TnsB-binding sites), and Tn7 also is functionally asymmetric, inserting into its specific target site, attachment site attTn7 (attTn7) in a single orientation. Moreover, Tn7 elements containing two Tn7 right ends can transpose, but elements with two Tn7 left ends cannot. We show here that TnsA + TnsB are unable to pair the ends of a Tn7 element containing two Tn7 left ends. This pairing defect likely contributes to the inability of Tn7 elements with two Tn7 left ends to transpose.
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