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.

Verrocchio, a Drosophila OB fold-containing protein, is a component of the terminin telomere-capping complex / Raffa, GRAZIA DANIELA; Raimondo, Domenico; Sorino, Chiarastella; Cugusi, Simona; Cenci, Giovanni; Cacchione, Stefano; Gatti, Maurizio; Ciapponi, Laura. - In: GENES & DEVELOPMENT. - ISSN 0890-9369. - STAMPA. - 24:15(2010), pp. 1596-1601. [10.1101/gad.574810]

Verrocchio, a Drosophila OB fold-containing protein, is a component of the terminin telomere-capping complex

RAFFA, GRAZIA DANIELA;RAIMONDO, Domenico;SORINO, Chiarastella;CUGUSI, SIMONA;CENCI, GIOVANNI;CACCHIONE, Stefano;GATTI, MAURIZIO;CIAPPONI, LAURA
2010

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.
2010
protein folding; protein structure; mutation; terminin; gene expression regulation; genetics/metabolism; chemistry/genetics/isolation /&/ purification/metabolism; tertiary; nuclear proteins; drosophila melanogaster; drosophila proteins; non-histone; telomeres; animals; drosophila; metabolism; chromosomal proteins; telomere; verrocchio; molecular; models; genetics; rpa2/stn1; protein binding; amino acid sequence; sequence alignment; telomere-binding proteins
01 Pubblicazione su rivista::01a Articolo in rivista
Verrocchio, a Drosophila OB fold-containing protein, is a component of the terminin telomere-capping complex / Raffa, GRAZIA DANIELA; Raimondo, Domenico; Sorino, Chiarastella; Cugusi, Simona; Cenci, Giovanni; Cacchione, Stefano; Gatti, Maurizio; Ciapponi, Laura. - In: GENES & DEVELOPMENT. - ISSN 0890-9369. - STAMPA. - 24:15(2010), pp. 1596-1601. [10.1101/gad.574810]
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Utilizza questo identificativo per citare o creare un link a questo documento: https://hdl.handle.net/11573/224463
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