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Immunofluorescent Staining for Visualization of Heterochromatin Associated Proteins in Drosophila Salivary Glands
Published on: August 21, 2021
Verrocchio, a Drosophila OB fold-containing protein, is a component of the terminin telomere-capping complex
Grazia D Raffa1, Domenico Raimondo, Cristina Sorino
1Dipartimento di Genetica e Biologia Molecolare Charles Darwin Sapienza, Università di Roma, Roma 00185, Italy.
Abstract:
Drosophila telomeres are elongated by transposition of specialized retroelements rather than telomerase activity, and are assembled independently of the terminal DNA sequence. Drosophila telomeres are protected by terminin, a complex that includes the HOAP (Heterochromatin Protein 1/origin recognition complex-associated protein) and Moi (Modigliani) proteins and shares the properties of human shelterin. Here we show that Verrocchio (Ver), an oligonucleotide/oligosaccharide-binding (OB) fold-containing protein related to Rpa2/Stn1, interacts physically with HOAP and Moi, is enriched only at telomeres, and prevents telomere fusion. These results indicate that Ver is a new terminin component; we speculate that, concomitant with telomerase loss, Drosophila evolved terminin to bind chromosome ends independently of the DNA sequence.
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