Interplay between Sae2 and Rif2 in the regulation of Mre11-Rad50 activities at DNA ends
Autor: | Diego Bonetti, Michela Clerici, Maria Pia Longhese |
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Přispěvatelé: | Bonetti, D, Clerici, M, Longhese, M |
Rok vydání: | 2021 |
Předmět: |
Saccharomyces cerevisiae Proteins
DNA Repair Saccharomyces cerevisiae Telomere-Binding Proteins BIO/18 - GENETICA Protein Serine-Threonine Kinases chemistry.chemical_compound Genetics Protein kinase A MRX/N Sae2 Rif2 DNA end chemistry.chemical_classification Endodeoxyribonucleases biology fungi Intracellular Signaling Peptides and Proteins Chromosome DNA biology.organism_classification Endonucleases Cell biology Telomere DNA-Binding Proteins enzymes and coenzymes (carbohydrates) Enzyme Exodeoxyribonucleases chemistry Rad50 biological phenomena cell phenomena and immunity Homologous recombination Developmental Biology |
Zdroj: | Current opinion in geneticsdevelopment. 71 |
ISSN: | 1879-0380 |
Popis: | DNA double-strand breaks (DSBs) can be repaired by non-homologous end-joining (NHEJ) or homologous recombination (HR). HR is initiated by nucleolytic degradation of the DSB ends in a process termed resection. The Mre11-Rad50-Xrs2/NBS1 (MRX/N) complex is a multifunctional enzyme that, aided by the Sae2/CtIP protein, promotes DSB resection and maintains the DSB ends tethered to each other to facilitate their re-ligation. Furthermore, it activates the protein kinase Tel1/ATM, which initiates DSB signaling. In Saccharomyces cerevisiae, these MRX functions are inhibited by the Rif2 protein, which is enriched at telomeres and protects telomeric DNA from being sensed and processed as a DSB. The present review focuses on recent data showing that Sae2 and Rif2 regulate MRX functions in opposite manners by interacting with Rad50 and influencing ATP-dependent Mre11-Rad50 conformational changes. As Sae2 is enriched at DSBs whereas Rif2 is predominantly present at telomeres, the relative abundance of these two MRX regulators can provide an effective mechanism to activate or inactivate MRX depending on the nature of chromosome ends. |
Databáze: | OpenAIRE |
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