ArticleNucleic acids research2007
Crystal structure of the left-handed archaeal RadA helical filament: identification of a functional motif for controlling quaternary structures and enzymatic functions of RecA family proteins.
Article in Nucleic acids research, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 papers.
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Who cites it
26 citing papers in PubMed, 42 citations in OpenAlex.
- Modeling the Homologous Recombination Process: Methods, Successes and Challenges.International journal of molecular sciences · 2023Review
- Divalent metal cofactors differentially modulate RadA-mediated strand invasion and exchange in Saccharolobus solfataricus.Bioscience reports · 2023Article
- A novel motif of Rad51 serves as an interaction hub for recombination auxiliary factors.eLife · 2021Article
- Protein splicing of a recombinase intein induced by ssDNA and DNA damage.Genes & development · 2016Article
- Article
- Post-translational environmental switch of RadA activity by extein-intein interactions in protein splicing.Nucleic acids research · 2015Article
- An integrative approach to the study of filamentous oligomeric assemblies, with application to RecA.PloS one · 2015Article
- Nanobiomotors of archaeal DNA repair machineries: current research status and application potential.Cell & bioscience · 2014Review
- An archaeal RadA paralog influences presynaptic filament formation.DNA repair · 2013Article
- Structure of a filament of stacked octamers of human DMC1 recombinase.Acta crystallographica. Section F, Structural biology and crystallization communications · 2013Article
- Mini-chromosome maintenance complexes form a filament to remodel DNA structure and topology.Nucleic acids research · 2013Article
- Oxidative stress in mammalian cells impinges on the cysteines redox state of human XRCC3 protein and on its cellular localization.PloS one · 2013Article
- Structure of a hexameric form of RadA recombinase from Methanococcus voltae.Acta crystallographica. Section F, Structural biology and crystallization communications · 2012Article
- A human XRCC4-XLF complex bridges DNA.Nucleic acids research · 2012Article
- Target molecular simulations of RecA family protein filaments.International journal of molecular sciences · 2012Article
- Thermodynamic Properties of Water Molecules at a Protein-Protein Interaction Surface.Journal of chemical theory and computation · 2011Article
- A rationally designed peptide enhances homologous recombination in vitro and resistance to DNA damaging agents in vivo.Nucleic acids research · 2010Article
- Bacteroides fragilis RecA protein overexpression causes resistance to metronidazole.Research in microbiology · 2010Article
- Article
- The N-terminal domain of Escherichia coli RecA have multiple functions in promoting homologous recombination.Journal of biomedical science · 2009Article
Corrections and comments
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Authors and funding
7 authors at 3 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The RecA family of proteins mediates homologous recombination, an evolutionarily conserved pathway that maintains genomic stability by protecting against DNA double strand breaks. RecA proteins are thought to facilitate DNA strand exchange reactions as closed-rings or as right-handed helical filaments. Here, we report the crystal structure of a left-handed Sulfolobus solfataricus RadA helical filament. Each protomer in this left-handed filament is linked to its neighbour via interactions of a beta-strand polymerization motif with the neighbouring ATPase domain. Immediately following the polymerization motif, we identified an evolutionarily conserved hinge region (a subunit rotation motif) in which a 360 degrees clockwise axial rotation accompanies stepwise structural transitions from a closed ring to the AMP-PNP right-handed filament, then to an overwound right-handed filament and finally to the left-handed filament. Additional structural and functional analyses of wild-type and mutant proteins confirmed that the subunit rotation motif is crucial for enzymatic functions of RecA family proteins. These observations support the hypothesis that RecA family protein filaments may function as rotary motors.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.