Natural chromosomal ends are stabilized by proteins that bind duplex t
elomeric DNA repeats. In human cells, the TTAGGG Repeat factor 1 (TRF1
) was identified by two independent studies, one screening for factors
that bind duplex telomeric DNA(1,2) and the other screening for prote
ins containing a particular Myb motif called the telobox, which is req
uired for telomeric repeat recognition (Fig. 1a; refs 3-5). A second h
uman open reading frame, orf2, contains a telobox sequence and encodes
a polypeptide that specifically recognizes mammalian telomeric repeat
DNA in vitro(3). We show that two proteins of 65 and 69 kD, expressed
in HeLa cells, contain the orf2 telobox sequence. These proteins are
collectively termed TRF2. Affinity-purified antibodies specific for an
ti-TRF2 label the telomeres of intact human chromosomes, strengthening
the correlation between occurrence of telobox and telomere-repeat rec
ognition in vivo.