ArticleNucleic acids research1998
Identification and characterization of the RAD51 gene from the ciliate Tetrahymena thermophila.
Article in Nucleic acids research, 1998. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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Who cites it
10 citing papers in PubMed, 26 citations in OpenAlex.
- Article
- A single cohesin complex performs mitotic and meiotic functions in the protist tetrahymena.PLoS genetics · 2013Article
- The recombinases Rad51 and Dmc1 play distinct roles in DNA break repair and recombination partner choice in the meiosis of Tetrahymena.PLoS genetics · 2011Article
- The evolution of meiosis from mitosis.Genetics · 2009Article
- DNA double-strand breaks, but not crossovers, are required for the reorganization of meiotic nuclei in Tetrahymena.Journal of cell science · 2008Article
- Transcriptional profile of the homologous recombination machinery and characterization of the EhRAD51 recombinase in response to DNA damage in Entamoeba histolytica.BMC molecular biology · 2008Article
- TIF1 activates the intra-S-phase checkpoint response in the diploid micronucleus and amitotic polyploid macronucleus of Tetrahymena.Molecular biology of the cell · 2006Article
- Transcriptional control of RAD51 expression in the ciliate Tetrahymena thermophila.Nucleic acids research · 2004Article
- The organization of Physcomitrella patensRAD51 genes is unique among eukaryotic organisms.Proceedings of the National Academy of Sciences of the United States of America · 2002Article
- Article
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
The RAD51 gene is a eukaryotic homolog of rec A, a critical component in homologous recombination and DNA repair pathways in Escherichia coli . We have cloned the RAD51 homolog from Tetrahymena thermophila , a ciliated protozoan. Tetrahymena thermophila RAD51 encodes a 36.3 kDa protein whose amino acid sequence is highly similar to representative Rad51 homologs from other eukaryotic taxa. Recombinant Rad51 protein was purified to near homogeneity following overproduction in a bacterial expression system. The purified protein binds to both single- and double-stranded DNA, possesses a DNA-dependent ATPase activity and promotes intermolecular ligation of linearized plasmid DNA. While steady-state levels of Rad51 mRNA are low in normally growing cells, treatment with UV light resulted in a >100-fold increase in mRNA levels. This increase in mRNA was time dependent, but relatively independent of UV dose over a range of 1400-5200 J/m2. Western blot analysis confirmed that Rad51 protein levels increase upon UV irradiation. Exposure to the alkylating agent methyl methane sulfonate also resulted in substantially elevated Rad51 protein levels in treated cells, with pronounced localization in the macronucleus. These data are consistent with the hypothesis that ciliates such as T.thermophila utilize a Rad51-dependent pathway to repair damaged DNA.
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