ArticleJournal of bacteriology2008
The stable, functional core of DdrA from Deinococcus radiodurans R1 does not restore radioresistance in vivo.
Article in Journal of bacteriology, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
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Who cites it
8 citing papers in PubMed, 15 citations in OpenAlex.
- DdrC, a unique DNA repair factor from D. radiodurans, senses and stabilizes DNA breaks through a novel lesion-recognition mechanism.Nucleic acids research · 2024Article
- Characterization of the DdrD protein from the extremely radioresistant bacterium Deinococcus radiodurans.Extremophiles : life under extreme conditions · 2021Article
- Construction, analysis and validation of co-expression network to understand stress adaptation in Deinococcus radiodurans R1.PloS one · 2020Article
- Oxidative stress response of Deinococcus geothermalis via a cystine importer.Journal of microbiology (Seoul, Korea) · 2017Article
- Biochemical characterization of RecA variants that contribute to extreme resistance to ionizing radiation.DNA repair · 2015Article
- Escherichia coli genes and pathways involved in surviving extreme exposure to ionizing radiation.Journal of bacteriology · 2014Article
- Purification, crystallization and preliminary X-ray diffraction analysis of DNA damage response A protein from Deinococcus radiodurans.Acta crystallographica. Section F, Structural biology and crystallization communications · 2010Article
- A new perspective on radiation resistance based on Deinococcus radiodurans.Nature reviews. Microbiology · 2009Review
Corrections and comments
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
DdrA protein binds to and protects 3' DNA ends and is essential for preserving the genome integrity of Deinococcus radiodurans following treatment by gamma radiation in an environment lacking nutrients. Limited proteolysis was used to identify a stable and functional protein core, designated DdrA157, consisting of the first 157 residues of the protein. In vitro, the biochemical differences between wild-type and mutant proteins were modest. DdrA exhibits a strong bias in binding DNA with 3' extensions but not with 5' extensions. The mutant DdrA157 exhibited a greater affinity for 5' DNA ends but still bound to 3' ends more readily. However, when we replaced the wild-type ddrA gene with the mutant gene for ddrA157, the resulting D. radiodurans strain became almost as sensitive to gamma radiation as the ddrA knockout strain. These results suggest that while the stable protein core DdrA157 is functional for DNA binding and protection assays in vitro, the carboxyl terminus is required for important functions in vivo. The C terminus may therefore be required for protein or DNA interactions or possibly as a regulatory region for DNA binding or activities not yet identified.
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Registered trials
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.