ArticleActa histochemica2011
Rad10-YFP focus induction in response to UV depends on RAD14 in yeast.
Article in Acta histochemica, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 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.
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Who cites it
7 citing papers in PubMed, 9 citations in OpenAlex.
- Growth Inhibition and DNA Damage Induced by X-Phenols in Yeast: A Quantitative Structure-Activity Relationship Study.ACS omega · 2017Article
- Sumoylation of the Rad1 nuclease promotes DNA repair and regulates its DNA association.Nucleic acids research · 2014Article
- Hrq1 facilitates nucleotide excision repair of DNA damage induced by 4-nitroquinoline-1-oxide and cisplatin in Saccharomyces cerevisiae.Journal of microbiology (Seoul, Korea) · 2014Article
- SAW1 is required for SDSA double-strand break repair in S. cerevisiae.Biochemical and biophysical research communications · 2014Article
- Rad51 ATP binding but not hydrolysis is required to recruit Rad10 in synthesis-dependent strand annealing sites inAdvances in biological chemistry · 2013Article
- Functional analysis of Rad14p, a DNA damage recognition factor in nucleotide excision repair, in regulation of transcription in vivo.The Journal of biological chemistry · 2013Article
- Rad7 E3 Ubiquitin Ligase Attenuates Polyubiquitylation of Rpn10 and Dsk2 Following DNA Damage inAdvances in biological chemistryArticle
Corrections and comments
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Authors and funding
6 authors at 1 institution in 1 country.
Funding
Abstract
Rad14 is a DNA damage recognition protein in yeast Nucleotide Excision Repair (NER) and believed to function early in the cascade of events. The function of Rad14 presumably precedes that of the Rad1-Rad10 endonuclease complex, which functions in a downstream step incising DNA 5' to the site of DNA damage. We investigated whether recruitment of Rad10 to UV-induced DNA damage sites in live cells is dependent on Rad14 using fluorescence microscopy. Experiments were carried out using Saccharomyces cerevisiae strains in which the gene for Rad14 was fused to Cyan Fluorescent Protein (Rad14-CFP) and that of Rad10 was fused to Yellow Fluorescent Protein (Rad10-YFP). Rad14-CFP forms nuclear localized CFP fluorescent foci in response to UV irradiation with the peak induction occurring 15min post-irradiation. In contrast, Rad10-YFP foci form in response to UV with the peak induction occurring 2h post-irradiation. Recruitment of Rad14-CFP is not dependent on the RAD10 gene but Rad10-YFP is recruited to UV-induced YFP foci in a RAD14-dependent fashion. Time-lapse experiments indicate that Rad14-CFP foci are transient, typically persisting less than 6min. Together these data support the model that yeast NER protein assembly is step-wise whereas Rad14 required to recruit Rad10 and Rad14 involvement is transient.
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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.