A shared docking motif in TRF1 and TRF2 used for differential recruitment of telomeric proteins

作者：Chen Yong; Yang Yuting; van Overbeek Megan; Donigian Jill R; Baciu Paul; de Lange Titia; Lei Ming^*

来源：Science, 2008, 319(5866): 1092-1096.

DOI：10.1126/science.1151804

Mammalian telomeres are protected by a six- protein complex: shelterin. Shelterin contains two closely related proteins ( TRF1 and TRF2), which recruit various proteins to telomeres. We dissect the interactions of TRF1 and TRF2 with their shared binding partner ( TIN2) and other shelterin accessory factors. TRF1 recognizes TIN2 using a conserved molecular surface in its TRF homology ( TRFH) domain. However, this same surface does not act as a TIN2 binding site in TRF2, and TIN2 binding to TRF2 is mediated by a region outside the TRFH domain. Instead, the TRFH docking site of TRF2 binds a shelterin accessory factor ( Apollo), which does not interact with the TRFH domain of TRF1. Conversely, the TRFH domain of TRF1, but not of TRF2, interacts with another shelterin- associated factor: PinX1.

• 出版日期2008-2-22