Mammalian Meiotic Telomeres: Protein Composition and Redistribution in Relation to Nuclear Pores
Document Type
Article
Publication Date
1-1-2000
Publication Title
Molecular Biology of the Cell
Disciplines
Biology
Abstract
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.
DOI
10.1091/mbc.11.12.4189
Recommended Citation
Scherthan, H.; Jerratsch, M.; Li, B.; Smith, S.; Hulten, M.; Lock, T.; and De Lange, T., "Mammalian Meiotic Telomeres: Protein Composition and Redistribution in Relation to Nuclear Pores" (2000). Biological, Geological, and Environmental Faculty Publications. 163.
https://engagedscholarship.csuohio.edu/scibges_facpub/163
Volume
11
Issue
12
Comments
These studies were supported by a Deutsche Forschungsgemeinschaft grant to H.S. (no.: Sche350/8–3). T.d.L. acknowledges grant support from the NIH. B.L. is a recipient of a fellowship from the Leukemia Society of America.