ArticleProceedings of the National Academy of Sciences of the United States of America2009
The Drosophila modigliani (moi) gene encodes a HOAP-interacting protein required for telomere protection.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 43 papers.
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Who cites it
43 citing papers in PubMed, 63 citations in OpenAlex.
- Convergence and conflict among telomere-specialized transposons across 60 million years of Drosophilid evolution.Genome research · 2026Article
- Rapid compensatory evolution within a multiprotein complex preserves telomere integrity.Science (New York, N.Y.) · 2025Article
- TGS1 impacts snRNA 3'-end processing, ameliorates survival motor neuron-dependent neurological phenotypes in vivo and prevents neurodegeneration.Nucleic acids research · 2022Article
- Mod(mdg4) variants repress telomeric retrotransposon HeT-A by blocking subtelomeric enhancers.Nucleic acids research · 2022Article
- Low dose rate γ-irradiation protects fruit fly chromosomes from double strand breaks and telomere fusions by reducing the esi-RNA biogenesis factor Loquacious.Communications biology · 2022Article
- Reduced Environmental Dose Rates Are Responsible for the Increased Susceptibility to Radiation-Induced DNA Damage in Larval Neuroblasts ofInternational journal of molecular sciences · 2022Article
- Evolutionary mode for the functional preservation of fast-evolvingOpen biology · 2021Article
- Taming active transposons at Drosophila telomeres: The interconnection between HipHop's roles in capping and transcriptional silencing.PLoS genetics · 2021Article
- Sequence, Chromatin and Evolution of Satellite DNA.International journal of molecular sciences · 2021Review
- Atomic Force Microscopy Reveals that the Drosophila Telomere-Capping Protein Verrocchio Is a Single-Stranded DNA-Binding Protein.Methods in molecular biology (Clifton, N.J.) · 2021Article
- Loss of the RNA trimethylguanosine cap is compatible with nuclear accumulation of spliceosomal snRNAs but not pre-mRNA splicing or snRNA processing during animal development.PLoS genetics · 2020Article
- Insights into HP1a-Chromatin Interactions.Cells · 2020Review
- Intimate functional interactions between TGS1 and the Smn complex revealed by an analysis of the Drosophila eye development.PLoS genetics · 2020Article
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- The Hybrid Incompatibility GenesGenetics · 2017Article
- Article
- Drosophila: Retrotransposons Making up Telomeres.Viruses · 2017Review
- The Drosophila telomere-capping protein Verrocchio binds single-stranded DNA and protects telomeres from DNA damage response.Nucleic acids research · 2017Article
- Life and cancer without telomerase: ALT and other strategies for making sure ends (don't) meet.Critical reviews in biochemistry and molecular biology · 2017Review
- Recurrent Innovation at Genes Required for Telomere Integrity in Drosophila.Molecular biology and evolution · 2017Article
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Authors and funding
7 authors at 4 institutions in 2 countries.
Funding
Abstract
Several proteins have been identified that protect Drosophila telomeres from fusion events. They include UbcD1, HP1, HOAP, the components of the Mre11-Rad50-Nbs (MRN) complex, the ATM kinase, and the putative transcription factor Woc. Of these proteins, only HOAP has been shown to localize specifically at telomeres. Here we show that the modigliani gene encodes a protein (Moi) that is enriched only at telomeres, colocalizes and physically interacts with HOAP, and is required to prevent telomeric fusions. Moi is encoded by the bicistronic CG31241 locus. This locus produces a single transcript that contains 2 ORFs that specify different essential functions. One of these ORFs encodes the 20-kDa Moi protein. The other encodes a 60-kDa protein homologous to RNA methyltransferases that is not required for telomere protection (Drosophila Tat-like). Moi and HOAP share several properties with the components of shelterin, the protein complex that protects human telomeres. HOAP and Moi are not evolutionarily conserved unlike the other proteins implicated in Drosophila telomere protection. Similarly, none of the shelterin subunits is conserved in Drosophila, while most human nonshelterin proteins have Drosophila homologues. This suggests that the HOAP-Moi complex, we name "terminin," plays a specific role in the DNA sequence-independent assembly of Drosophila telomeres. We speculate that this complex is functionally analogous to shelterin, which binds chromosome ends in a sequence-dependent manner.
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