Bacterial RadA is a DnaB-type helicase interacting with RecA to promote bidirectional D-loop extension
| Autor: | Marie, Léa, Rapisarda, Chiara, Morales, Violette, Bergé, Mathieu, Perry, Thomas, Soulet, Anne-Lise, Gruget, Clémence, Remaut, Han, Fronzes, Rémi, Polard, Patrice |
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| Přispěvatelé: | Structural Biology Brussels, Department of Bio-engineering Sciences |
| Jazyk: | angličtina |
| Rok vydání: | 2017 |
| Předmět: |
Recombination
Genetic Science DNA Helicases DNA Single-Stranded Crystallography X-Ray Article DNA-Binding Proteins Rec A Recombinases Streptococcus pneumoniae Bacterial Proteins Protein Domains Two-Hybrid System Techniques Mutagenesis Site-Directed bacteria Homologous Recombination Protein Structure Quaternary DnaB Helicases |
| Zdroj: | Nature Communications, Vol 8, Iss 1, Pp 1-14 (2017) 'Nature Communications ', vol: 8, pages: 15638-1-15638-14 (2017) Nature Communications |
| ISSN: | 2041-1723 |
| Popis: | Homologous recombination (HR) is a central process of genome biology driven by a conserved recombinase, which catalyses the pairing of single-stranded DNA (ssDNA) with double-stranded DNA to generate a D-loop intermediate. Bacterial RadA is a conserved HR effector acting with RecA recombinase to promote ssDNA integration. The mechanism of this RadA-mediated assistance to RecA is unknown. Here, we report functional and structural analyses of RadA from the human pathogen Streptococcus pneumoniae. RadA is found to facilitate RecA-driven ssDNA recombination over long genomic distances during natural transformation. RadA is revealed as a hexameric DnaB-type helicase, which interacts with RecA to promote orientated unwinding of branched DNA molecules mimicking D-loop boundaries. These findings support a model of DNA branch migration in HR, relying on RecA-mediated loading of RadA hexamers on each strand of the recipient dsDNA in the D-loop, from which they migrate divergently to facilitate incorporation of invading ssDNA. Bacterial homologous recombination involves the actions of RadA and RecA to promote single-stranded DNA integration. Here the authors report the structure of RadA from Streptococcus pneumoniae and demonstrate that it acts as a hexameric DnaB-type helicase. |
| Databáze: | OpenAIRE |
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