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Published Online January 17, 2008
Science DOI: 10.1126/science.1151804

Reports

Submitted on October 16, 2007
Accepted on January 7, 2008

A Shared Docking Motif in TRF1 and TRF2 Used for Differential Recruitment of Telomeric Proteins

Yong Chen 1, Yuting Yang 1, Megan van Overbeek 2{dagger}, Jill R. Donigian 2{dagger}, Paul Baciu 1, Titia de Lange 2, Ming Lei 1*

1 Department of Biological Chemistry, University of Michigan Medical School, 1500 W. Medical Center Drive, Ann Arbor, MI 48109, USA.
2 Laboratory for Cell Biology and Genetics, The Rockefeller University, 1230 York Avenue, New York, NY 10065, USA.

* To whom correspondence should be addressed.
Ming Lei , E-mail: leim{at}umich.edu

{dagger}These authors contributed equally to this work.

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. Here 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.


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Science. ISSN 0036-8075 (print), 1095-9203 (online)