ArticlePloS one2007
Structural and functional analyses of five conserved positively charged residues in the L1 and N-terminal DNA binding motifs of archaeal RADA protein.
Article in PloS one, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
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Who cites it
11 citing papers in PubMed, 20 citations in OpenAlex.
- RAD51 and Infertility: A Review and Case-Control Study.Biochemical genetics · 2024Review
- The Lon protease-like domain in the bacterial RecA paralog RadA is required for DNA binding and repair.The Journal of biological chemistry · 2017Article
- Nanobiomotors of archaeal DNA repair machineries: current research status and application potential.Cell & bioscience · 2014Review
- A rationally designed peptide enhances homologous recombination in vitro and resistance to DNA damaging agents in vivo.Nucleic acids research · 2010Article
- Article
- Structural and functional characterisation of a conserved archaeal RadA paralog with antirecombinase activity.Journal of molecular biology · 2009Article
- DIDS, a chemical compound that inhibits RAD51-mediated homologous pairing and strand exchange.Nucleic acids research · 2009Article
- The N-terminal domain of Escherichia coli RecA have multiple functions in promoting homologous recombination.Journal of biomedical science · 2009Article
- Article
- An improved SUMO fusion protein system for effective production of native proteins.Protein science : a publication of the Protein Society · 2008Article
- Structural and functional analyses of the DMC1-M200V polymorphism found in the human population.Nucleic acids research · 2008Article
Corrections and comments
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Authors and funding
6 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
RecA family proteins engage in an ATP-dependent DNA strand exchange reaction that includes a ssDNA nucleoprotein helical filament and a homologous dsDNA sequence. In spite of more than 20 years of efforts, the molecular mechanism of homology pairing and strand exchange is still not fully understood. Here we report a crystal structure of Sulfolobus solfataricus RadA overwound right-handed filament with three monomers per helical pitch. This structure reveals conformational details of the first ssDNA binding disordered loop (denoted L1 motif) and the dsDNA binding N-terminal domain (NTD). L1 and NTD together form an outwardly open palm structure on the outer surface of the helical filament. Inside this palm structure, five conserved basic amino acid residues (K27, K60, R117, R223 and R229) surround a 25 A pocket that is wide enough to accommodate anionic ssDNA, dsDNA or both. Biochemical analyses demonstrate that these five positively charged residues are essential for DNA binding and for RadA-catalyzed D-loop formation. We suggest that the overwound right-handed RadA filament represents a functional conformation in the homology search and pairing reaction. A new structural model is proposed for the homologous interactions between a RadA-ssDNA nucleoprotein filament and its dsDNA target.
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