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Molecular architecture of the SYCP3 fibre and its interaction with DNA

The synaptonemal complex (SC) keeps homologous chromosomes in close alignment during meiotic recombination. A hallmark of the SC is the presence of its constituent protein SYCP3 on the chromosome axis. During SC assembly, SYCP3 is deposited on both axes of the homologue pair, forming axial elements...

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Autores principales: Bollschweiler, Daniel, Radu, Laura, Joudeh, Luay, Plitzko, Jürgen M., Henderson, Robert M., Mela, Ioanna, Pellegrini, Luca
Formato: Online Artículo Texto
Lenguaje:English
Publicado: The Royal Society 2019
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6833220/
https://www.ncbi.nlm.nih.gov/pubmed/31615332
http://dx.doi.org/10.1098/rsob.190094
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author Bollschweiler, Daniel
Radu, Laura
Joudeh, Luay
Plitzko, Jürgen M.
Henderson, Robert M.
Mela, Ioanna
Pellegrini, Luca
author_facet Bollschweiler, Daniel
Radu, Laura
Joudeh, Luay
Plitzko, Jürgen M.
Henderson, Robert M.
Mela, Ioanna
Pellegrini, Luca
author_sort Bollschweiler, Daniel
collection PubMed
description The synaptonemal complex (SC) keeps homologous chromosomes in close alignment during meiotic recombination. A hallmark of the SC is the presence of its constituent protein SYCP3 on the chromosome axis. During SC assembly, SYCP3 is deposited on both axes of the homologue pair, forming axial elements that fuse into the lateral element (LE) in the tripartite structure of the mature SC. We have used cryo-electron tomography and atomic force microscopy to study the mechanism of assembly and DNA binding of the SYCP3 fibre. We find that the three-dimensional architecture of the fibre is built on a highly irregular arrangement of SYCP3 molecules displaying very limited local geometry. Interaction between SYCP3 molecules is driven by the intrinsically disordered tails of the protein, with no contact between the helical cores, resulting in a flexible fibre assembly. We demonstrate that the SYCP3 fibre can engage in extensive interactions with DNA, indicative of an efficient mechanism for incorporation of DNA within the fibre. Our findings suggest that SYCP3 deposition on the chromosome axis might take place by polymerization into a fibre that is fastened to the chromosome surface via DNA binding.
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spelling pubmed-68332202019-11-12 Molecular architecture of the SYCP3 fibre and its interaction with DNA Bollschweiler, Daniel Radu, Laura Joudeh, Luay Plitzko, Jürgen M. Henderson, Robert M. Mela, Ioanna Pellegrini, Luca Open Biol Research The synaptonemal complex (SC) keeps homologous chromosomes in close alignment during meiotic recombination. A hallmark of the SC is the presence of its constituent protein SYCP3 on the chromosome axis. During SC assembly, SYCP3 is deposited on both axes of the homologue pair, forming axial elements that fuse into the lateral element (LE) in the tripartite structure of the mature SC. We have used cryo-electron tomography and atomic force microscopy to study the mechanism of assembly and DNA binding of the SYCP3 fibre. We find that the three-dimensional architecture of the fibre is built on a highly irregular arrangement of SYCP3 molecules displaying very limited local geometry. Interaction between SYCP3 molecules is driven by the intrinsically disordered tails of the protein, with no contact between the helical cores, resulting in a flexible fibre assembly. We demonstrate that the SYCP3 fibre can engage in extensive interactions with DNA, indicative of an efficient mechanism for incorporation of DNA within the fibre. Our findings suggest that SYCP3 deposition on the chromosome axis might take place by polymerization into a fibre that is fastened to the chromosome surface via DNA binding. The Royal Society 2019-10-16 /pmc/articles/PMC6833220/ /pubmed/31615332 http://dx.doi.org/10.1098/rsob.190094 Text en © 2019 The Authors. http://creativecommons.org/licenses/by/4.0/ Published by the Royal Society under the terms of the Creative Commons Attribution License http://creativecommons.org/licenses/by/4.0/, which permits unrestricted use, provided the original author and source are credited.
spellingShingle Research
Bollschweiler, Daniel
Radu, Laura
Joudeh, Luay
Plitzko, Jürgen M.
Henderson, Robert M.
Mela, Ioanna
Pellegrini, Luca
Molecular architecture of the SYCP3 fibre and its interaction with DNA
title Molecular architecture of the SYCP3 fibre and its interaction with DNA
title_full Molecular architecture of the SYCP3 fibre and its interaction with DNA
title_fullStr Molecular architecture of the SYCP3 fibre and its interaction with DNA
title_full_unstemmed Molecular architecture of the SYCP3 fibre and its interaction with DNA
title_short Molecular architecture of the SYCP3 fibre and its interaction with DNA
title_sort molecular architecture of the sycp3 fibre and its interaction with dna
topic Research
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6833220/
https://www.ncbi.nlm.nih.gov/pubmed/31615332
http://dx.doi.org/10.1098/rsob.190094
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