Cargando…
A suppressor screen in C. elegans identifies a multi-protein interaction interface that stabilizes the synaptonemal complex
Successful chromosome segregation into gametes depends on tightly-regulated interactions between the parental chromosomes. During meiosis, chromosomes are aligned end-to-end by an interface called the synaptonemal complex, which also regulates exchanges between them. However, despite the functional...
Autores principales: | , , |
---|---|
Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Cold Spring Harbor Laboratory
2023
|
Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC10473659/ https://www.ncbi.nlm.nih.gov/pubmed/37662357 http://dx.doi.org/10.1101/2023.08.21.554166 |
_version_ | 1785100316920774656 |
---|---|
author | Kursel, Lisa E. Martinez, Jesus E. Aguayo Rog, Ofer |
author_facet | Kursel, Lisa E. Martinez, Jesus E. Aguayo Rog, Ofer |
author_sort | Kursel, Lisa E. |
collection | PubMed |
description | Successful chromosome segregation into gametes depends on tightly-regulated interactions between the parental chromosomes. During meiosis, chromosomes are aligned end-to-end by an interface called the synaptonemal complex, which also regulates exchanges between them. However, despite the functional and ultrastructural conservation of this essential interface, how protein-protein interactions within the synaptonemal complex regulate chromosomal interactions remains poorly understood. Here we describe a novel interaction interface in the C. elegans synaptonemal complex, comprised of short segments of three proteins, SYP-1, SYP-3 and SYP-4. We identified the interface through a saturated suppressor screen of a mutant that destabilizes the synaptonemal complex. The specificity and tight distribution of suppressors point to a charge-based interface that promotes interactions between synaptonemal complex subunits and, in turn, allows intimate interactions between chromosomes. Our work highlights the power of genetic studies to illuminate the mechanisms that underly meiotic chromosome interactions. |
format | Online Article Text |
id | pubmed-10473659 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2023 |
publisher | Cold Spring Harbor Laboratory |
record_format | MEDLINE/PubMed |
spelling | pubmed-104736592023-09-02 A suppressor screen in C. elegans identifies a multi-protein interaction interface that stabilizes the synaptonemal complex Kursel, Lisa E. Martinez, Jesus E. Aguayo Rog, Ofer bioRxiv Article Successful chromosome segregation into gametes depends on tightly-regulated interactions between the parental chromosomes. During meiosis, chromosomes are aligned end-to-end by an interface called the synaptonemal complex, which also regulates exchanges between them. However, despite the functional and ultrastructural conservation of this essential interface, how protein-protein interactions within the synaptonemal complex regulate chromosomal interactions remains poorly understood. Here we describe a novel interaction interface in the C. elegans synaptonemal complex, comprised of short segments of three proteins, SYP-1, SYP-3 and SYP-4. We identified the interface through a saturated suppressor screen of a mutant that destabilizes the synaptonemal complex. The specificity and tight distribution of suppressors point to a charge-based interface that promotes interactions between synaptonemal complex subunits and, in turn, allows intimate interactions between chromosomes. Our work highlights the power of genetic studies to illuminate the mechanisms that underly meiotic chromosome interactions. Cold Spring Harbor Laboratory 2023-08-22 /pmc/articles/PMC10473659/ /pubmed/37662357 http://dx.doi.org/10.1101/2023.08.21.554166 Text en https://creativecommons.org/licenses/by-nc/4.0/This work is licensed under a Creative Commons Attribution-NonCommercial 4.0 International License (https://creativecommons.org/licenses/by-nc/4.0/) , which allows reusers to distribute, remix, adapt, and build upon the material in any medium or format for noncommercial purposes only, and only so long as attribution is given to the creator. |
spellingShingle | Article Kursel, Lisa E. Martinez, Jesus E. Aguayo Rog, Ofer A suppressor screen in C. elegans identifies a multi-protein interaction interface that stabilizes the synaptonemal complex |
title | A suppressor screen in C. elegans identifies a multi-protein interaction interface that stabilizes the synaptonemal complex |
title_full | A suppressor screen in C. elegans identifies a multi-protein interaction interface that stabilizes the synaptonemal complex |
title_fullStr | A suppressor screen in C. elegans identifies a multi-protein interaction interface that stabilizes the synaptonemal complex |
title_full_unstemmed | A suppressor screen in C. elegans identifies a multi-protein interaction interface that stabilizes the synaptonemal complex |
title_short | A suppressor screen in C. elegans identifies a multi-protein interaction interface that stabilizes the synaptonemal complex |
title_sort | suppressor screen in c. elegans identifies a multi-protein interaction interface that stabilizes the synaptonemal complex |
topic | Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC10473659/ https://www.ncbi.nlm.nih.gov/pubmed/37662357 http://dx.doi.org/10.1101/2023.08.21.554166 |
work_keys_str_mv | AT kursellisae asuppressorscreenincelegansidentifiesamultiproteininteractioninterfacethatstabilizesthesynaptonemalcomplex AT martinezjesuseaguayo asuppressorscreenincelegansidentifiesamultiproteininteractioninterfacethatstabilizesthesynaptonemalcomplex AT rogofer asuppressorscreenincelegansidentifiesamultiproteininteractioninterfacethatstabilizesthesynaptonemalcomplex AT kursellisae suppressorscreenincelegansidentifiesamultiproteininteractioninterfacethatstabilizesthesynaptonemalcomplex AT martinezjesuseaguayo suppressorscreenincelegansidentifiesamultiproteininteractioninterfacethatstabilizesthesynaptonemalcomplex AT rogofer suppressorscreenincelegansidentifiesamultiproteininteractioninterfacethatstabilizesthesynaptonemalcomplex |