The non-homologous end-joining protein Nej1p is a target of the DNA damage checkpoint
| Autor: | Peter Ahnesorg, Stephen P. Jackson |
|---|---|
| Rok vydání: | 2007 |
| Předmět: |
Saccharomyces cerevisiae Proteins
DNA Repair DNA repair DNA damage Molecular Sequence Data Cell Cycle Proteins Saccharomyces cerevisiae Protein Serine-Threonine Kinases Biology Biochemistry Article Serine DNA Breaks Double-Stranded Amino Acid Sequence CHEK1 Phosphorylation Molecular Biology Cell Nucleus Recombination Genetic chemistry.chemical_classification DNA ligase Binding Sites Sequence Homology Amino Acid Genetic Complementation Test Intracellular Signaling Peptides and Proteins Cell Biology G2-M DNA damage checkpoint DNA repair protein XRCC4 Molecular biology Recombinant Proteins DNA-Binding Proteins Non-homologous end joining Checkpoint Kinase 2 enzymes and coenzymes (carbohydrates) Amino Acid Substitution chemistry Mutagenesis Site-Directed Homologous recombination Protein Kinases Signal Transduction |
| Zdroj: | DNA Repair. 6:190-201 |
| ISSN: | 1568-7864 |
| DOI: | 10.1016/j.dnarep.2006.09.010 |
| Popis: | DNA double-strand breaks (DSBs), which are generated by ionizing radiation (IR) and a range of other DNA damaging agents, are repaired by homologous recombination (HR) or non-homologous end-joining (NHEJ). Previous studies have shown that NHEJ in Saccharomyces cerevisiae requires the Yku70p–Yku80p heterodimer and a complex consisting of DNA Ligase IV, Lif1p and Nej1p. Here, we report that Nej1p is phosphorylated in response to DNA damage in a manner that relies on the DNA damage checkpoint kinases Mec1p, Rad53p and Dun1p. By using a mutational approach, we have identified a consensus Dun1p phosphorylation site in Nej1p, and mutation of conserved serine residues within it leads to decreased NHEJ efficiency. These data, together with previous findings that Rad55p – a protein involved in HR – is phosphorylated analogously, point to there being a broad signalling network connecting DNA damage checkpoint responses with the regulation of DNA DSB repair activities. |
| Databáze: | OpenAIRE |
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