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Title: The protein network surrounding the human telomere repeat binding factors TRF1, TRF2, and POT1

Journal Article · · PLoS ONE
 [1];  [2];  [1];  [3]
  1. ORNL
  2. National Institute on Aging, National Institutes of Health
  3. National Institute on Aging, Baltimore

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.

Research Organization:
Oak Ridge National Lab. (ORNL), Oak Ridge, TN (United States)
Sponsoring Organization:
USDOE Laboratory Directed Research and Development (LDRD) Program; USDOE Office of Science (SC)
DOE Contract Number:
DE-AC05-00OR22725
OSTI ID:
986421
Journal Information:
PLoS ONE, Vol. 5, Issue 8; ISSN 1932-6203
Country of Publication:
United States
Language:
English