The Rtf1/Prf1-dependent histone modification axis counteracts multi-drug resistance in fission yeast.
Journal
Life science alliance
ISSN: 2575-1077
Titre abrégé: Life Sci Alliance
Pays: United States
ID NLM: 101728869
Informations de publication
Date de publication:
Jun 2024
Jun 2024
Historique:
received:
26
11
2023
revised:
05
03
2024
accepted:
06
03
2024
medline:
22
3
2024
pubmed:
22
3
2024
entrez:
21
3
2024
Statut:
epublish
Résumé
RNA polymerase II transcription elongation directs an intricate pattern of histone modifications. This pattern includes a regulatory cascade initiated by the elongation factor Rtf1, leading to monoubiquitylation of histone H2B, and subsequent methylation of histone H3 on lysine 4. Previous studies have defined the molecular basis for these regulatory relationships, but it remains unclear how they regulate gene expression. To address this question, we investigated a drug resistance phenotype that characterizes defects in this axis in the model eukaryote
Identifiants
pubmed: 38514187
pii: 7/6/e202302494
doi: 10.26508/lsa.202302494
pii:
doi:
Types de publication
Journal Article
Langues
eng
Sous-ensembles de citation
IM
Informations de copyright
© 2024 Chen et al.