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Structural basis of meiotic telomere attachment to the nuclear envelope by MAJIN-TERB2-TERB1
Meiotic chromosomes undergo rapid prophase movements, which are thought to facilitate the formation of inter-homologue recombination intermediates that underlie synapsis, crossing over and segregation. The meiotic telomere complex (MAJIN, TERB1, TERB2) tethers telomere ends to the nuclear envelope a...
Autores principales: | , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Nature Publishing Group UK
2018
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6297230/ https://www.ncbi.nlm.nih.gov/pubmed/30559341 http://dx.doi.org/10.1038/s41467-018-07794-7 |
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author | Dunce, James M. Milburn, Amy E. Gurusaran, Manickam da Cruz, Irene Sen, Lee T. Benavente, Ricardo Davies, Owen R. |
author_facet | Dunce, James M. Milburn, Amy E. Gurusaran, Manickam da Cruz, Irene Sen, Lee T. Benavente, Ricardo Davies, Owen R. |
author_sort | Dunce, James M. |
collection | PubMed |
description | Meiotic chromosomes undergo rapid prophase movements, which are thought to facilitate the formation of inter-homologue recombination intermediates that underlie synapsis, crossing over and segregation. The meiotic telomere complex (MAJIN, TERB1, TERB2) tethers telomere ends to the nuclear envelope and transmits cytoskeletal forces via the LINC complex to drive these rapid movements. Here, we report the molecular architecture of the meiotic telomere complex through the crystal structure of MAJIN-TERB2, together with light and X-ray scattering studies of wider complexes. The MAJIN-TERB2 2:2 hetero-tetramer binds strongly to DNA and is tethered through long flexible linkers to the inner nuclear membrane and two TRF1-binding 1:1 TERB2-TERB1 complexes. Our complementary structured illumination microscopy studies and biochemical findings reveal a telomere attachment mechanism in which MAJIN-TERB2-TERB1 recruits telomere-bound TRF1, which is then displaced during pachytene, allowing MAJIN-TERB2-TERB1 to bind telomeric DNA and form a mature attachment plate. |
format | Online Article Text |
id | pubmed-6297230 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2018 |
publisher | Nature Publishing Group UK |
record_format | MEDLINE/PubMed |
spelling | pubmed-62972302018-12-19 Structural basis of meiotic telomere attachment to the nuclear envelope by MAJIN-TERB2-TERB1 Dunce, James M. Milburn, Amy E. Gurusaran, Manickam da Cruz, Irene Sen, Lee T. Benavente, Ricardo Davies, Owen R. Nat Commun Article Meiotic chromosomes undergo rapid prophase movements, which are thought to facilitate the formation of inter-homologue recombination intermediates that underlie synapsis, crossing over and segregation. The meiotic telomere complex (MAJIN, TERB1, TERB2) tethers telomere ends to the nuclear envelope and transmits cytoskeletal forces via the LINC complex to drive these rapid movements. Here, we report the molecular architecture of the meiotic telomere complex through the crystal structure of MAJIN-TERB2, together with light and X-ray scattering studies of wider complexes. The MAJIN-TERB2 2:2 hetero-tetramer binds strongly to DNA and is tethered through long flexible linkers to the inner nuclear membrane and two TRF1-binding 1:1 TERB2-TERB1 complexes. Our complementary structured illumination microscopy studies and biochemical findings reveal a telomere attachment mechanism in which MAJIN-TERB2-TERB1 recruits telomere-bound TRF1, which is then displaced during pachytene, allowing MAJIN-TERB2-TERB1 to bind telomeric DNA and form a mature attachment plate. Nature Publishing Group UK 2018-12-17 /pmc/articles/PMC6297230/ /pubmed/30559341 http://dx.doi.org/10.1038/s41467-018-07794-7 Text en © The Author(s) 2018 Open Access This article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license, and indicate if changes were made. The images or other third party material in this article are included in the article’s Creative Commons license, unless indicated otherwise in a credit line to the material. If material is not included in the article’s Creative Commons license and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this license, visit http://creativecommons.org/licenses/by/4.0/. |
spellingShingle | Article Dunce, James M. Milburn, Amy E. Gurusaran, Manickam da Cruz, Irene Sen, Lee T. Benavente, Ricardo Davies, Owen R. Structural basis of meiotic telomere attachment to the nuclear envelope by MAJIN-TERB2-TERB1 |
title | Structural basis of meiotic telomere attachment to the nuclear envelope by MAJIN-TERB2-TERB1 |
title_full | Structural basis of meiotic telomere attachment to the nuclear envelope by MAJIN-TERB2-TERB1 |
title_fullStr | Structural basis of meiotic telomere attachment to the nuclear envelope by MAJIN-TERB2-TERB1 |
title_full_unstemmed | Structural basis of meiotic telomere attachment to the nuclear envelope by MAJIN-TERB2-TERB1 |
title_short | Structural basis of meiotic telomere attachment to the nuclear envelope by MAJIN-TERB2-TERB1 |
title_sort | structural basis of meiotic telomere attachment to the nuclear envelope by majin-terb2-terb1 |
topic | Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6297230/ https://www.ncbi.nlm.nih.gov/pubmed/30559341 http://dx.doi.org/10.1038/s41467-018-07794-7 |
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