title: Mammalian meiotic telomeres: protein composition and redistribution in relation to nuclear pores.
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.
authors: University of Kaiserslautern, D-67653 Kaiserslautern, Germany. scherth@rhrk.uni-kl.de
authors: H
authors: H
authors: Scherthan
authors: M
authors: M
authors: Jerratsch
authors: B
authors: B
authors: Li
authors: S
authors: S
authors: Smith
authors: M
authors: M
authors: Hultén
authors: T
authors: T
authors: Lock
authors: T
authors: T
authors: de Lange
mesh_terms: D000818:Animals; D002875:Chromosomes / Q000648:ultrastructure; D004268:DNA-Binding Proteins / Q000276:immunology / Q000378:metabolism; D019084:Fluorescent Antibody Technique, Indirect; D006801:Humans; D008297:Male; D008540:Meiosis; D051379:Mice; D022022:Nuclear Pore / Q000378:metabolism*; D011065:Poly(ADP-ribose) Polymerases / Q000276:immunology / Q000378:metabolism; D011418:Prophase; D051381:Rats; D000089804:Shelterin Complex; D013090:Spermatocytes / Q000166:cytology / Q000378:metabolism; D038501:Tankyrases; D016615:Telomere / Q000737:chemistry* / Q000378:metabolism*; D034501:Telomere-Binding Proteins; D035321:Telomeric Repeat Binding Protein 1; D035341:Telomeric Repeat Binding Protein 2; D020827:rap1 GTP-Binding Proteins / Q000276:immunology / Q000378:metabolism
chemical_list: D004268:DNA-Binding Proteins; D011065:Poly(ADP-ribose) Polymerases; D000089804:Shelterin Complex; D038501:Tankyrases; D034501:Telomere-Binding Proteins; D035321:Telomeric Repeat Binding Protein 1; D035341:Telomeric Repeat Binding Protein 2; D020827:rap1 GTP-Binding Proteins; C440809:TERF2IP protein, human; C498822:Tnks protein, mouse; C418109:TNKS protein, human