Unconventional conservation reveals structure-function relationships in the synaptonemal complex

Functional requirements constrain protein evolution, commonly manifesting in a conserved amino acid sequence. Here, we extend this idea to secondary structural features by tracking their conservation in essential meiotic proteins with highly diverged sequences. The synaptonemal complex (SC) is a ~10...

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Autores principales: Lisa E Kursel, Henry D Cope, Ofer Rog
Formato: article
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Publicado: eLife Sciences Publications Ltd 2021
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Acceso en línea:https://doaj.org/article/bc16d92a8a5a42d0b4692e96904a7b5b
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spelling oai:doaj.org-article:bc16d92a8a5a42d0b4692e96904a7b5b2021-11-24T12:24:08ZUnconventional conservation reveals structure-function relationships in the synaptonemal complex10.7554/eLife.720612050-084Xe72061https://doaj.org/article/bc16d92a8a5a42d0b4692e96904a7b5b2021-11-01T00:00:00Zhttps://elifesciences.org/articles/72061https://doaj.org/toc/2050-084XFunctional requirements constrain protein evolution, commonly manifesting in a conserved amino acid sequence. Here, we extend this idea to secondary structural features by tracking their conservation in essential meiotic proteins with highly diverged sequences. The synaptonemal complex (SC) is a ~100-nm-wide ladder-like meiotic structure present in all eukaryotic clades, where it aligns parental chromosomes and regulates exchanges between them. Despite the conserved ultrastructure and functions of the SC, SC proteins are highly divergent within Caenorhabditis. However, SC proteins have highly conserved length and coiled-coil domain structure. We found the same unconventional conservation signature in Drosophila and mammals, and used it to identify a novel SC protein in Pristionchus pacificus, Ppa-SYP-1. Our work suggests that coiled-coils play wide-ranging roles in the structure and function of the SC, and more broadly, that expanding sequence analysis beyond measures of per-site similarity can enhance our understanding of protein evolution and function.Lisa E KurselHenry D CopeOfer RogeLife Sciences Publications LtdarticleP. pacificusmeiosissynaptonemal complexcoiled-coilindelevolutionMedicineRScienceQBiology (General)QH301-705.5ENeLife, Vol 10 (2021)
institution DOAJ
collection DOAJ
language EN
topic P. pacificus
meiosis
synaptonemal complex
coiled-coil
indel
evolution
Medicine
R
Science
Q
Biology (General)
QH301-705.5
spellingShingle P. pacificus
meiosis
synaptonemal complex
coiled-coil
indel
evolution
Medicine
R
Science
Q
Biology (General)
QH301-705.5
Lisa E Kursel
Henry D Cope
Ofer Rog
Unconventional conservation reveals structure-function relationships in the synaptonemal complex
description Functional requirements constrain protein evolution, commonly manifesting in a conserved amino acid sequence. Here, we extend this idea to secondary structural features by tracking their conservation in essential meiotic proteins with highly diverged sequences. The synaptonemal complex (SC) is a ~100-nm-wide ladder-like meiotic structure present in all eukaryotic clades, where it aligns parental chromosomes and regulates exchanges between them. Despite the conserved ultrastructure and functions of the SC, SC proteins are highly divergent within Caenorhabditis. However, SC proteins have highly conserved length and coiled-coil domain structure. We found the same unconventional conservation signature in Drosophila and mammals, and used it to identify a novel SC protein in Pristionchus pacificus, Ppa-SYP-1. Our work suggests that coiled-coils play wide-ranging roles in the structure and function of the SC, and more broadly, that expanding sequence analysis beyond measures of per-site similarity can enhance our understanding of protein evolution and function.
format article
author Lisa E Kursel
Henry D Cope
Ofer Rog
author_facet Lisa E Kursel
Henry D Cope
Ofer Rog
author_sort Lisa E Kursel
title Unconventional conservation reveals structure-function relationships in the synaptonemal complex
title_short Unconventional conservation reveals structure-function relationships in the synaptonemal complex
title_full Unconventional conservation reveals structure-function relationships in the synaptonemal complex
title_fullStr Unconventional conservation reveals structure-function relationships in the synaptonemal complex
title_full_unstemmed Unconventional conservation reveals structure-function relationships in the synaptonemal complex
title_sort unconventional conservation reveals structure-function relationships in the synaptonemal complex
publisher eLife Sciences Publications Ltd
publishDate 2021
url https://doaj.org/article/bc16d92a8a5a42d0b4692e96904a7b5b
work_keys_str_mv AT lisaekursel unconventionalconservationrevealsstructurefunctionrelationshipsinthesynaptonemalcomplex
AT henrydcope unconventionalconservationrevealsstructurefunctionrelationshipsinthesynaptonemalcomplex
AT oferrog unconventionalconservationrevealsstructurefunctionrelationshipsinthesynaptonemalcomplex
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