ArticleJournal of bacteriology2002
RecA Protein from the extremely radioresistant bacterium Deinococcus radiodurans: expression, purification, and characterization.
Article in Journal of bacteriology, 2002. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 32 papers.
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Who cites it
32 citing papers in PubMed, 78 citations in OpenAlex.
- Recombinase-Controlled Multiphase Condensates Accelerate Nucleic Acid Amplification and CRISPR-Based Diagnostics.Journal of the American Chemical Society · 2025Article
- Raiding nature's genetic toolbox for UV-C resistance by functional metagenomics.Scientific reports · 2025Article
- The regulation mechanism of the C-terminus of RecA proteins during DNA strand-exchange process.Biophysical journal · 2021Article
- DNA Damage Protection for Enhanced Bacterial Survival Under Simulated Low Earth Orbit Environmental Conditions inFrontiers in microbiology · 2021Article
- Single-Molecule Insights into ATP-Dependent Conformational Dynamics of Nucleoprotein Filaments ofInternational journal of molecular sciences · 2020Article
- Influence of the C-Terminal Tail of RecA Proteins from Alkaline pH-Resistant BacteriumACS omega · 2020Article
- Functional Division Between the RecA1 and RecA2 Proteins inFrontiers in microbiology · 2020Article
- Conservation and diversity of radiation and oxidative stress resistance mechanisms in Deinococcus species.FEMS microbiology reviews · 2019Review
- Radiation resistance in thermophiles: mechanisms and applications.World journal of microbiology & biotechnology · 2017Review
- The cohesin-like RecN protein stimulates RecA-mediated recombinational repair of DNA double-strand breaks.Nature communications · 2017Article
- The DnaE polymerase from Deinococcus radiodurans features RecA-dependent DNA polymerase activity.Bioscience reports · 2016Article
- Phosphorylation of Deinococcus radiodurans RecA Regulates Its Activity and May Contribute to Radioresistance.The Journal of biological chemistry · 2016Article
- A Decade of Biochemical and Structural Studies of the DNA Repair Machinery ofComputational and structural biotechnology journal · 2016Review
- Article
- Transcriptional analysis of Deinococcus radiodurans reveals novel small RNAs that are differentially expressed under ionizing radiation.Applied and environmental microbiology · 2015Article
- Functional roles of N-terminal and C-terminal domains in the overall activity of a novel single-stranded DNA binding protein of Deinococcus radiodurans.FEBS open bio · 2015Article
- DR1769, a protein with N-terminal beta propeller repeats and a low-complexity hydrophilic tail, plays a role in desiccation tolerance of Deinococcus radiodurans.Journal of bacteriology · 2013Article
- Regulation of Deinococcus radiodurans RecA protein function via modulation of active and inactive nucleoprotein filament states.The Journal of biological chemistry · 2013Article
- Regulation of MntH by a dual Mn(II)- and Fe(II)-dependent transcriptional repressor (DR2539) in Deinococcus radiodurans.PloS one · 2012Article
- Investigating Deinococcus radiodurans RecA protein filament formation on double-stranded DNA by a real-time single-molecule approach.Biochemistry · 2011Article
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Authors and funding
10 authors at 2 institutions in 1 country.
Funding
Abstract
The RecA protein of Deinococcus radiodurans (RecA(Dr)) is essential for the extreme radiation resistance of this organism. The RecA(Dr) protein has been cloned and expressed in Escherichia coli and purified from this host. In some respects, the RecA(Dr) protein and the E. coli RecA (RecA(Ec)) proteins are close functional homologues. RecA(Dr) forms filaments on single-stranded DNA (ssDNA) that are similar to those formed by the RecA(Ec). The RecA(Dr) protein hydrolyzes ATP and dATP and promotes DNA strand exchange reactions. DNA strand exchange is greatly facilitated by the E. coli SSB protein. As is the case with the E. coli RecA protein, the use of dATP as a cofactor permits more facile displacement of bound SSB protein from ssDNA. However, there are important differences as well. The RecA(Dr) protein promotes ATP- and dATP-dependent reactions with distinctly different pH profiles. Although dATP is hydrolyzed at approximately the same rate at pHs 7.5 and 8.1, dATP supports an efficient DNA strand exchange only at pH 8.1. At both pHs, ATP supports efficient DNA strand exchange through heterologous insertions but dATP does not. Thus, dATP enhances the binding of RecA(Dr) protein to ssDNA and the displacement of ssDNA binding protein, but the hydrolysis of dATP is poorly coupled to DNA strand exchange. The RecA(Dr) protein thus may offer new insights into the role of ATP hydrolysis in the DNA strand exchange reactions promoted by the bacterial RecA proteins. In addition, the RecA(Dr) protein binds much better to duplex DNA than the RecA(Ec) protein, binding preferentially to double-stranded DNA (dsDNA) even when ssDNA is present in the solutions. This may be of significance in the pathways for dsDNA break repair in Deinococcus.
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