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

Journal article
Authors Jingjing Zhang
Zhaowei Tu
Yoshinori Watanabe
Hiroki Shibuya
Published in Cell reports
Volume 21
Issue 7
Pages 1715-1726
ISSN 2211-1247
Publication year 2017
Published at Department of Chemistry and Molecular Biology
Pages 1715-1726
Language en
Links dx.doi.org/10.1016/j.celrep.2017.10...
www.ncbi.nlm.nih.gov/entrez/query.f...
Subject categories Cell Biology

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.

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