Abstract
Telomere integrity (including telomere length and capping) is critical in overall genomic stability. Telomere repeat binding
factors and their associated proteins play vital roles in telomere length regulation and end protection. In this study, we
explore the protein network surrounding telomere repeat binding factors, TRF1, TRF2, and POT1 using dual-tag affinity
purification in combination with multidimensional protein identification technology liquid chromatography - tandem mass
spectrometry (MudPIT LC-MS/MS). After control subtraction and data filtering, we found that TRF2 and POT1 co-purified all
six members of the telomere protein complex, while TRF1 identified five of six components at frequencies that lend
evidence towards the currently accepted telomere architecture. Many of the known TRF1 or TRF2 interacting proteins were
also identified. Moreover, putative associating partners identified for each of the three core components fell into functional
categories such as DNA damage repair, ubiquitination, chromosome cohesion, chromatin modification/remodeling, DNA
replication, cell cycle and transcription regulation, nucleotide metabolism, RNA processing, and nuclear transport. These
putative protein-protein associations may participate in different biological processes at telomeres or, intriguingly, outside
telomeres.
