To investigate the interplay between TRF2 and telomeric chromatin, we infected human cancer cell (C33A from cervix) with lentiviral vectors encoding TRF2 full-length or a truncated form which lacked both the N-terminal basic domain and the telobox Myb-like C-terminal DNA-binding domain (TRF2ΔBΔM); this mutant has a dominant negative activity, since it forms dimers with TRF2 that have a reduced ability to bind telomeres [25]. The gene discussed is TERF2; the disease is cancer.