Narya, a RING finger domain-containing protein, is required for meiotic DNA double-strand break formation and crossover maturation in Drosophila melanogaster
Autor: | Amanda M. Bonner, Kim S. McKim, Rachel J. Nielsen, Cathleen M. Lake, R. Scott Hawley, Sanese K. White-Brown, Salam Eche |
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Rok vydání: | 2019 |
Předmět: |
Cancer Research
QH426-470 Biochemistry Chromosomal crossover chemistry.chemical_compound RNA interference 0302 clinical medicine Animal Cells Yeast Two-Hybrid Assays DNA Breaks Double-Stranded Crossing Over Genetic Cell Cycle and Cell Division Homologous Recombination Genetics (clinical) 0303 health sciences Sex Chromosomes Chromosome Biology Drosophila Melanogaster Eukaryota X Chromosomes Animal Models Cell biology Insects Nucleic acids RING finger domain Meiosis medicine.anatomical_structure Experimental Organism Systems Genetic interference Cell Processes OVA Drosophila Epigenetics Cellular Types RING Finger Domains Protein Interaction Assays Research Article X Chromosome Arthropoda DNA recombination Protein domain Meiotic DNA double-strand break formation Biology Research and Analysis Methods Chromosomes 03 medical and health sciences Model Organisms Protein Domains Two-Hybrid System Techniques Genetics Ring finger medicine Animals Molecular Biology Techniques Molecular Biology Ecology Evolution Behavior and Systematics 030304 developmental biology Molecular Biology Assays and Analysis Techniques fungi Organisms Biology and Life Sciences Proteins Cell Biology DNA Invertebrates Germ Cells chemistry Oocytes Animal Studies RNA Gene expression Homologous recombination 030217 neurology & neurosurgery |
Zdroj: | PLoS Genetics PLoS Genetics, Vol 15, Iss 1, p e1007886 (2019) |
ISSN: | 1553-7404 |
Popis: | Meiotic recombination, which is necessary to ensure that homologous chromosomes segregate properly, begins with the induction of meiotic DNA double-strand breaks (DSBs) and ends with the repair of a subset of those breaks into crossovers. Here we investigate the roles of two paralogous genes, CG12200 and CG31053, which we have named Narya and Nenya, respectively, due to their relationship with a structurally similar protein named Vilya. We find that narya recently evolved from nenya by a gene duplication event, and we show that these two RING finger domain-containing proteins are functionally redundant with respect to a critical role in DSB formation. Narya colocalizes with Vilya foci, which are known to define recombination nodules, or sites of crossover formation. A separation-of-function allele of narya retains the capacity for DSB formation but cannot mature those DSBs into crossovers. We further provide data on the physical interaction of Narya, Nenya and Vilya, as assayed by the yeast two-hybrid system. Together these data support the view that all three RING finger domain-containing proteins function in the formation of meiotic DNA DSBs and in the process of crossing over. Author summary Errors in chromosome segregation during meiosis are the leading cause of miscarriages and can result in genetic abnormalities like Down syndrome or Turner syndrome. For chromosomes to segregate faithfully, they must recombine with their homolog during the early steps of meiosis. An essential component of the process of meiotic recombination is creating the lesions (double-strand breaks, DSBs) that are required to form a crossover with the homologous chromosome. Crossovers are required to ensure chromosomes segregate properly at the first meiotic division. In this study we have identified two genes, narya and nenya, that are essential in DSB formation. We found that narya arose from a duplication of nenya, and these two genes are functionally redundant. In addition to its role in DSB formation, narya also plays a role in processing DSBs into crossovers. Strengthening our knowledge about the mechanism by which Narya both creates DSBs and processes them into crossovers will lead to a better understanding of the process of meiotic chromosome segregation not only in flies but many other organisms, as these genes have homologs in yeast, worms, plants, mice and humans. |
Databáze: | OpenAIRE |
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