Drosophila telomere capping protein HOAP interacts with DSB sensor proteins Mre11 and Nbs

In eukaryotes, specific DNA‐protein structures called telomeres exist at linear chromosome ends. Telomere stability is maintained by a specific capping protein complex. This capping complex is essential for the inhibition of the DNA damage response (DDR) at telomeres and contributes to genome integrity. In Drosophila, the central factors of telomere capping complex are HOAP and HipHop. Furthermore, a DDR protein complex Mre11‐Rad50‐Nbs (MRN) is known to be important for the telomere association of HOAP and HipHop. However, whether MRN interacts with HOAP and HipHop, and the telomere recognition mechanisms of HOAP and HipHop are poorly understood. Here, we show that Nbs interacts with Mre11 and transports the Mre11‐Rad50 complex from the cytoplasm to the nucleus. In addition, we report that HOAP interacts with both Mre11 and Nbs. The N‐terminal region of HOAP is essential for its co‐localization with HipHop. Finally, we reveal that Nbs interacts with the N‐terminal region of HOAP. In Drosophila, a DNA damage response protein complex Mre11‐Rad50‐Nbs (MRN) is known to be important for the telomere association of HOAP and HipHop. However, whether MRN interacts with HOAP and HipHop, and the telomere recognition mechanisms of HOAP and HipHop are poorly understood. In this study, we reveal that the N‐terminal region of HOAP is essential for its co‐localization with HipHop and its interaction with Nbs.