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IS21 family transposase cleaved donor complex traps two right-handed superhelical crossings

Author

Listed:
  • Mercedes Spínola-Amilibia

    (Centro de Investigaciones Biológicas Margarita Salas, CSIC)

  • Lidia Araújo-Bazán

    (Centro de Investigaciones Biológicas Margarita Salas, CSIC)

  • Álvaro Gándara

    (Centro de Investigaciones Biológicas Margarita Salas, CSIC)

  • James M. Berger

    (Johns Hopkins University School of Medicine)

  • Ernesto Arias-Palomo

    (Centro de Investigaciones Biológicas Margarita Salas, CSIC)

Abstract

Transposases are ubiquitous enzymes that catalyze DNA rearrangement events with broad impacts on gene expression, genome evolution, and the spread of drug-resistance in bacteria. Here, we use biochemical and structural approaches to define the molecular determinants by which IstA, a transposase present in the widespread IS21 family of mobile elements, catalyzes efficient DNA transposition. Solution studies show that IstA engages the transposon terminal sequences to form a high-molecular weight complex and promote DNA integration. A 3.4 Å resolution structure of the transposase bound to transposon ends corroborates our biochemical findings and reveals that IstA self-assembles into a highly intertwined tetramer that synapses two supercoiled terminal inverted repeats. The three-dimensional organization of the IstA•DNA cleaved donor complex reveals remarkable similarities with retroviral integrases and classic transposase systems, such as Tn7 and bacteriophage Mu, and provides insights into IS21 transposition.

Suggested Citation

  • Mercedes Spínola-Amilibia & Lidia Araújo-Bazán & Álvaro Gándara & James M. Berger & Ernesto Arias-Palomo, 2023. "IS21 family transposase cleaved donor complex traps two right-handed superhelical crossings," Nature Communications, Nature, vol. 14(1), pages 1-14, December.
    • Handle: RePEc:nat:natcom:v:14:y:2023:i:1:d:10.1038_s41467-023-38071-x
    DOI: 10.1038/s41467-023-38071-x
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    References listed on IDEAS

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    1. Christian Biémont & Cristina Vieira, 2006. "Junk DNA as an evolutionary force," Nature, Nature, vol. 443(7111), pages 521-524, October.
    2. Jung-Un Park & Amy Wei-Lun Tsai & Alexandrea N. Rizo & Vinh H. Truong & Tristan X. Wellner & Richard D. Schargel & Elizabeth H. Kellogg, 2023. "Structures of the holo CRISPR RNA-guided transposon integration complex," Nature, Nature, vol. 613(7945), pages 775-782, January.
    3. Stephen Hare & Saumya Shree Gupta & Eugene Valkov & Alan Engelman & Peter Cherepanov, 2010. "Retroviral intasome assembly and inhibition of DNA strand transfer," Nature, Nature, vol. 464(7286), pages 232-236, March.
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