An interchangeable prion-like domain is required for Ty1 retrotransposition.
Journal
bioRxiv : the preprint server for biology
Titre abrégé: bioRxiv
Pays: United States
ID NLM: 101680187
Informations de publication
Date de publication:
27 Feb 2023
27 Feb 2023
Historique:
entrez:
13
3
2023
pubmed:
14
3
2023
medline:
14
3
2023
Statut:
epublish
Résumé
Retrotransposons and retroviruses shape genome evolution and can negatively impact genome function. Retrovirus-like retrotransposons help shape the genome evolution of their hosts and replicate within cytoplasmic particles. How their building blocks associate and assemble within the cell is poorly understood. Here, we report a novel pr ion-like d omain (PrLD) in the budding yeast retrotransposon Ty1 Gag protein that builds virus-like particles. The PrLD has similar sequence properties to prions and disordered protein domains that can drive the formation of assemblies that range from liquid to solid. We demonstrate that the Ty1 PrLD can function as a prion and that certain prion sequences can replace the PrLD and support Ty1 transposition. This interchangeable system is an effective platform to study additional disordered sequences in living cells.
Identifiants
pubmed: 36909481
doi: 10.1101/2023.02.27.530227
pmc: PMC10002725
pii:
doi:
Types de publication
Preprint
Langues
eng
Commentaires et corrections
Type : UpdateIn
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