Unconventional conservation reveals structure-function relationships in the synaptonemal complex.
C. elegans
D. melanogaster
P. pacificus
coiled-coil
evolution
evolutionary biology
genetics
genomics
human
indel
meiosis
synaptonemal complex
Journal
eLife
ISSN: 2050-084X
Titre abrégé: Elife
Pays: England
ID NLM: 101579614
Informations de publication
Date de publication:
17 11 2021
17 11 2021
Historique:
received:
08
07
2021
accepted:
21
10
2021
entrez:
17
11
2021
pubmed:
18
11
2021
medline:
15
12
2021
Statut:
epublish
Résumé
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
Identifiants
pubmed: 34787570
doi: 10.7554/eLife.72061
pii: 72061
pmc: PMC8598163
doi:
pii:
Types de publication
Journal Article
Research Support, N.I.H., Extramural
Langues
eng
Sous-ensembles de citation
IM
Subventions
Organisme : NIGMS NIH HHS
ID : R35 GM128804
Pays : United States
Organisme : NIH HHS
ID : P40 OD010440
Pays : United States
Organisme : NICHD NIH HHS
ID : T32 HD007491
Pays : United States
Informations de copyright
© 2021, Kursel et al.
Déclaration de conflit d'intérêts
LK, HC, OR No competing interests declared
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