ArticleNucleic acids research2015
Loop L1 governs the DNA-binding specificity and order for RecA-catalyzed reactions in homologous recombination and DNA repair.
Article in Nucleic acids research, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.
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16 citing papers in PubMed, 26 citations in OpenAlex.
- Mechanistic insights into the structure and function of the RecA C-terminal tail.Communications biology · 2026Article
- Quantitative Evaluation of Endogenous Reference Genes for RT-qPCR and ddPCR Gene Expression Under Polyextreme Conditions Using Anaerobic Halophilic AlkalithermophileMicroorganisms · 2025Article
- Plasticity and Co-Factor-Dependent Structural Changes in the RecA Nucleoprotein Filament Studied by Small-Angle X-Ray Scattering (SAXS) Measurements and Molecular Modeling.Molecules (Basel, Switzerland) · 2025Article
- Homology recognition without double-stranded DNA-strand separation in D-loop formation by RecA.Nucleic acids research · 2024Article
- Engineered RecA Constructs Reveal the Minimal SOS Activation Complex.Biochemistry · 2022Article
- Mechanisms of distinctive mismatch tolerance between Rad51 and Dmc1 in homologous recombination.Nucleic acids research · 2021Article
- The regulation mechanism of the C-terminus of RecA proteins during DNA strand-exchange process.Biophysical journal · 2021Article
- Structural insights into the inhibition of bacterial RecA by naphthalene polysulfonated compounds.iScience · 2021Article
- The intrinsic ability of double-stranded DNA to carry out D-loop and R-loop formation.Computational and structural biotechnology journal · 2020Review
- Computational elucidation of the binding mechanisms of curcumin analogues as bacterial RecA inhibitors.RSC advances · 2019Article
- Nonfilament-forming RecA dimer catalyzes homologous joint formation.Nucleic acids research · 2018Article
- Blocking the RecA activity and SOS-response in bacteria with a short α-helical peptide.Nucleic acids research · 2017Article
- The Lon protease-like domain in the bacterial RecA paralog RadA is required for DNA binding and repair.The Journal of biological chemistry · 2017Article
- Rad51 and RecA juxtapose dsDNA ends ready for DNA ligase-catalyzed end-joining under recombinase-suppressive conditions.Nucleic acids research · 2017Article
- Cryo-EM structures of human RAD51 recombinase filaments during catalysis of DNA-strand exchange.Nature structural & molecular biology · 2017Article
- Deinococcus radiodurans pprI expression enhances the radioresistance of eukaryotes.Oncotarget · 2016Article
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Authors and funding
9 authors at 3 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
In all organisms, RecA-family recombinases catalyze homologous joint formation in homologous genetic recombination, which is essential for genome stability and diversification. In homologous joint formation, ATP-bound RecA/Rad51-recombinases first bind single-stranded DNA at its primary site and then interact with double-stranded DNA at another site. The underlying reason and the regulatory mechanism for this conserved binding order remain unknown. A comparison of the loop L1 structures in a DNA-free RecA crystal that we originally determined and in the reported DNA-bound active RecA crystals suggested that the aspartate at position 161 in loop L1 in DNA-free RecA prevented double-stranded, but not single-stranded, DNA-binding to the primary site. This was confirmed by the effects of the Ala-replacement of Asp-161 (D161A), analyzed directly by gel-mobility shift assays and indirectly by DNA-dependent ATPase activity and SOS repressor cleavage. When RecA/Rad51-recombinases interact with double-stranded DNA before single-stranded DNA, homologous joint-formation is suppressed, likely by forming a dead-end product. We found that the D161A-replacement reduced this suppression, probably by allowing double-stranded DNA to bind preferentially and reversibly to the primary site. Thus, Asp-161 in the flexible loop L1 of wild-type RecA determines the preference for single-stranded DNA-binding to the primary site and regulates the DNA-binding order in RecA-catalyzed recombinase reactions.
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