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Micro-homology intermediates: RecA's transient sampling revealed at the single molecule level.
Lee, Andrew J; Endo, Masayuki; Hobbs, Jamie K; Davies, A Giles; Wälti, Christoph.
Afiliación
  • Lee AJ; Bioelectronics, The Pollard Institute, School of Electronic and Electrical Engineering, University of Leeds, Woodhouse lane, Leeds LS2 9JT, UK.
  • Endo M; Institute for Integrated Cell-Material Sciences, Kyoto University, Yoshida-ushinomiyacho, Sakyo-ku, Kyoto 606-8501, Japan.
  • Hobbs JK; Department of Physics and Astronomy, University of Sheffield, Houndsfield Road, Sheffield S3 7RH, UK.
  • Davies AG; Bioelectronics, The Pollard Institute, School of Electronic and Electrical Engineering, University of Leeds, Woodhouse lane, Leeds LS2 9JT, UK.
  • Wälti C; Bioelectronics, The Pollard Institute, School of Electronic and Electrical Engineering, University of Leeds, Woodhouse lane, Leeds LS2 9JT, UK.
Nucleic Acids Res ; 49(3): 1426-1435, 2021 02 22.
Article en En | MEDLINE | ID: mdl-33476368
Recombinase A (RecA) is central to homologous recombination. However, despite significant advances, the mechanism with which RecA is able to orchestrate a search for homology remains elusive. DNA nanostructure-augmented high-speed AFM offers the spatial and temporal resolutions required to study the RecA recombination mechanism directly and at the single molecule level. We present the direct in situ observation of RecA-orchestrated alignment of homologous DNA strands to form a stable recombination product within a supporting DNA nanostructure. We show the existence of subtle and short-lived states in the interaction landscape, which suggests that RecA transiently samples micro-homology at the single RecA monomer-level throughout the search for sequence alignment. These transient interactions form the early steps in the search for sequence homology, prior to the formation of stable pairings at >8 nucleotide seeds. The removal of sequence micro-homology results in the loss of the associated transient sampling at that location.
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Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Rec A Recombinasas / Proteínas de Escherichia coli / Proteínas de Unión al ADN / Recombinación Homóloga Idioma: En Revista: Nucleic Acids Res Año: 2021 Tipo del documento: Article Pais de publicación: Reino Unido
Texto completo
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XML
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Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Rec A Recombinasas / Proteínas de Escherichia coli / Proteínas de Unión al ADN / Recombinación Homóloga Idioma: En Revista: Nucleic Acids Res Año: 2021 Tipo del documento: Article Pais de publicación: Reino Unido