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Cell Rep. 2017 Nov 14;21(7):1715-1726. doi: 10.1016/j.celrep.2017.10.061.

Distinct TERB1 Domains Regulate Different Protein Interactions in Meiotic Telomere Movement.

Author information

1
Department of Chemistry and Molecular Biology, University of Gothenburg, 40530 Gothenburg, Sweden.
2
Laboratory of Chromosome Dynamics, Institute of Molecular and Cellular Biosciences, University of Tokyo, 1-1-1 Yayoi, Tokyo 113-0032, Japan.
3
Department of Chemistry and Molecular Biology, University of Gothenburg, 40530 Gothenburg, Sweden. Electronic address: hiroki.shibuya@gu.se.

Abstract

Meiotic telomeres attach to the nuclear envelope (NE) and drive the chromosome movement required for the pairing of homologous chromosomes. The meiosis-specific telomere proteins TERB1, TERB2, and MAJIN are required to regulate these events, but their assembly processes are largely unknown. Here, we developed a germ-cell-specific knockout mouse of the canonical telomere-binding protein TRF1 and revealed an essential role for TRF1 in directing the assembly of TERB1-TERB2-MAJIN. Further, we identified a TERB2 binding (T2B) domain in TERB1 that is dispensable for the TRF1-TERB1 interaction but is essential for the subsequent TERB1-TERB2 interaction and therefore for telomere attachment to the NE. Meanwhile, cohesin recruitment at telomeres, which is required for efficient telomere movement, is mediated by the MYB-like domain of TERB1, but not by TERB2-MAJIN. Our results reveal distinct protein interactions through various domains of TERB1, which enable the sequential assembly of the meiotic telomere complex for their movements.

KEYWORDS:

MAJIN; TERB1; TERB2; TRF1; chromosome; germ cell; meiosis; shelterin; telomere

PMID:
29141207
DOI:
10.1016/j.celrep.2017.10.061
[Indexed for MEDLINE]
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