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Short-range translocation by a restriction enzyme motor triggers diffusion along DNA.
Göse, Martin; Magill, Emma E; Hughes-Games, Alex; Shaw, Steven J; Diffin, Fiona M; Rawson, Tara; Nagy, Zsofia; Seidel, Ralf; Szczelkun, Mark D.
Afiliación
  • Göse M; Peter Debye Institute for Soft Matter Physics, Universität Leipzig, Leipzig, Germany.
  • Magill EE; DNA-Protein Interactions Unit, School of Biochemistry, University of Bristol, Bristol, UK.
  • Hughes-Games A; DNA-Protein Interactions Unit, School of Biochemistry, University of Bristol, Bristol, UK.
  • Shaw SJ; DNA-Protein Interactions Unit, School of Biochemistry, University of Bristol, Bristol, UK.
  • Diffin FM; DNA-Protein Interactions Unit, School of Biochemistry, University of Bristol, Bristol, UK.
  • Rawson T; DNA-Protein Interactions Unit, School of Biochemistry, University of Bristol, Bristol, UK.
  • Nagy Z; DNA-Protein Interactions Unit, School of Biochemistry, University of Bristol, Bristol, UK.
  • Seidel R; Peter Debye Institute for Soft Matter Physics, Universität Leipzig, Leipzig, Germany. ralf.seidel@physik.uni-leipzig.de.
  • Szczelkun MD; DNA-Protein Interactions Unit, School of Biochemistry, University of Bristol, Bristol, UK. mark.szczelkun@bristol.ac.uk.
Nat Chem Biol ; 20(6): 689-698, 2024 Jun.
Article en En | MEDLINE | ID: mdl-38167920
ABSTRACT
Cleavage of bacteriophage DNA by the Type III restriction-modification enzymes requires long-range interaction between DNA sites. This is facilitated by one-dimensional diffusion ('DNA sliding') initiated by ATP hydrolysis catalyzed by a superfamily 2 helicase-like ATPase. Here we combined ultrafast twist measurements based on plasmonic DNA origami nano-rotors with stopped-flow fluorescence and gel-based assays to examine the role(s) of ATP hydrolysis. Our data show that the helicase-like domain has multiple roles. First, this domain stabilizes initial DNA interactions alongside the methyltransferase subunits. Second, it causes environmental changes in the flipped adenine base following hydrolysis of the first ATP. Finally, it remodels nucleoprotein interactions via constrained translocation of a ∼ 5 to 22-bp double stranded DNA loop. Initiation of DNA sliding requires 8-15 bp of DNA downstream of the motor, corresponding to the site of nuclease domain binding. Our data unify previous contradictory communication models for Type III enzymes.
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Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Adenosina Trifosfato Idioma: En Revista: Nat Chem Biol Asunto de la revista: BIOLOGIA / QUIMICA Año: 2024 Tipo del documento: Article País de afiliación: Alemania Pais de publicación: Estados Unidos
Texto completo
Añadir a Mi BVS
Imprimir
XML
PubMed Links
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Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Adenosina Trifosfato Idioma: En Revista: Nat Chem Biol Asunto de la revista: BIOLOGIA / QUIMICA Año: 2024 Tipo del documento: Article País de afiliación: Alemania Pais de publicación: Estados Unidos