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Vol. 11, Issue 12, 4189-4203, December 2000
*University of Kaiserslautern, D-67653 Kaiserslautern,
Germany; Mammalian telomeres consist of TTAGGG repeats, telomeric repeat
binding factor (TRF), and other proteins, resulting in a protective structure at chromosome ends. Although structure and function of the
somatic telomeric complex has been elucidated in some detail, the
protein composition of mammalian meiotic telomeres is undetermined. Here we show, by indirect immunofluorescence (IF), that the meiotic telomere complex is similar to its somatic counterpart and contains significant amounts of TRF1, TRF2, and hRap1, while tankyrase, a
poly-(ADP-ribose)polymerase at somatic telomeres and nuclear pores,
forms small signals at ends of human meiotic chromosome cores. Analysis
of rodent spermatocytes reveals Trf1 at mouse, TRF2 at rat, and
mammalian Rap1 at meiotic telomeres of both rodents. Moreover, we
demonstrate that telomere repositioning during meiotic prophase occurs
in sectors of the nuclear envelope that are distinct from nuclear
pore-dense areas. The latter form during preleptotene/leptotene and are
present during entire prophase I.
Rockefeller Univiversity, New York, New York
10032; University Hospital, Utrecht, the Netherlands;
§University of Warwick, United Kingdom
Current address: Skirball Institute of
Biomolecular Medicine, New York University School of Medicine, 540 First Avenue, New York, NY 10016.
¶
Corresponding author. E-mail:
scherth{at}rhrk.uni-kl.de
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