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The large bat Helitron DNA transposase forms a compact monomeric assembly that buries and protects its covalently bound 5'-transposon end.
Kosek, Dalibor; Grabundzija, Ivana; Lei, Haotian; Bilic, Ilija; Wang, Huaibin; Jin, Yukun; Peaslee, Graham F; Hickman, Alison B; Dyda, Fred.
Afiliación
  • Kosek D; Laboratory of Molecular Biology, National Institute of Diabetes and Digestive and Kidney Diseases, National Institutes of Health, Bethesda, MD 20892, USA.
  • Grabundzija I; Laboratory of Molecular Biology, National Institute of Diabetes and Digestive and Kidney Diseases, National Institutes of Health, Bethesda, MD 20892, USA; BioNTech Cell & Gene Therapies GmbH, 55131 Mainz, Germany.
  • Lei H; Laboratory of Molecular Biology, National Institute of Diabetes and Digestive and Kidney Diseases, National Institutes of Health, Bethesda, MD 20892, USA.
  • Bilic I; BioNTech Cell & Gene Therapies GmbH, 55131 Mainz, Germany.
  • Wang H; Multi-Institute Cryo-Electron Microscopy Facility, National Institute of Diabetes and Digestive and Kidney Diseases, National Institutes of Health, Bethesda, MD 20892, USA.
  • Jin Y; Department of Physics, University of Notre Dame, Notre Dame, IN 46556, USA.
  • Peaslee GF; Department of Physics, University of Notre Dame, Notre Dame, IN 46556, USA.
  • Hickman AB; Laboratory of Molecular Biology, National Institute of Diabetes and Digestive and Kidney Diseases, National Institutes of Health, Bethesda, MD 20892, USA.
  • Dyda F; Laboratory of Molecular Biology, National Institute of Diabetes and Digestive and Kidney Diseases, National Institutes of Health, Bethesda, MD 20892, USA. Electronic address: fred.dyda@nih.gov.
Mol Cell ; 81(20): 4271-4286.e4, 2021 10 21.
Article en En | MEDLINE | ID: mdl-34403695
Helitrons are widespread eukaryotic DNA transposons that have significantly contributed to genome variability and evolution, in part because of their distinctive, replicative rolling-circle mechanism, which often mobilizes adjacent genes. Although most eukaryotic transposases form oligomers and use RNase H-like domains to break and rejoin double-stranded DNA (dsDNA), Helitron transposases contain a single-stranded DNA (ssDNA)-specific HUH endonuclease domain. Here, we report the cryo-electron microscopy structure of a Helitron transposase bound to the 5'-transposon end, providing insight into its multidomain architecture and function. The monomeric transposase forms a tightly packed assembly that buries the covalently attached cleaved end, protecting it until the second end becomes available. The structure reveals unexpected architectural similarity to TraI, a bacterial relaxase that also catalyzes ssDNA movement. The HUH active site suggests how two juxtaposed tyrosines, a feature of many replication initiators that use HUH nucleases, couple the conformational shift of an α-helix to control strand cleavage and ligation reactions.
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Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: ADN de Cadena Simple / Elementos Transponibles de ADN / Quirópteros / Transposasas Límite: Animals / Humans Idioma: En Revista: Mol Cell Asunto de la revista: BIOLOGIA MOLECULAR Año: 2021 Tipo del documento: Article País de afiliación: Estados Unidos Pais de publicación: Estados Unidos
Texto completo
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Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: ADN de Cadena Simple / Elementos Transponibles de ADN / Quirópteros / Transposasas Límite: Animals / Humans Idioma: En Revista: Mol Cell Asunto de la revista: BIOLOGIA MOLECULAR Año: 2021 Tipo del documento: Article País de afiliación: Estados Unidos Pais de publicación: Estados Unidos