Transcriptional activation domains interact with ATPase subunits of yeast chromatin remodelling complexes SWI/SNF, RSC and INO80.
Saccharomyces cerevisiae Proteins
/ genetics
Adenosine Triphosphatases
/ genetics
Transcription Factors
/ genetics
Saccharomyces cerevisiae
/ genetics
Chromatin Assembly and Disassembly
/ genetics
DNA-Binding Proteins
/ genetics
Transcriptional Activation
Protein Binding
Chromosomal Proteins, Non-Histone
/ genetics
Gene Expression Regulation, Fungal
Protein Domains
Nuclear Proteins
Cell Cycle Proteins
Basic Helix-Loop-Helix Transcription Factors
Saccharomyces cerevisiae
Activation domains
Activator binding domain
Chromatin remodelling complex
Ino80
Sth1
Swi2
Journal
Current genetics
ISSN: 1432-0983
Titre abrégé: Curr Genet
Pays: United States
ID NLM: 8004904
Informations de publication
Date de publication:
05 Sep 2024
05 Sep 2024
Historique:
received:
11
06
2024
accepted:
07
08
2024
revised:
25
07
2024
medline:
5
9
2024
pubmed:
5
9
2024
entrez:
5
9
2024
Statut:
epublish
Résumé
Chromatin remodelling complexes (CRC) are ATP-dependent molecular machines important for the dynamic organization of nucleosomes along eukaryotic DNA. CRCs SWI/SNF, RSC and INO80 can move positioned nucleosomes in promoter DNA, leading to nucleosome-depleted regions which facilitate access of general transcription factors. This function is strongly supported by transcriptional activators being able to interact with subunits of various CRCs. In this work we show that SWI/SNF subunits Swi1, Swi2, Snf5 and Snf6 can bind to activation domains of Ino2 required for expression of phospholipid biosynthetic genes in yeast. We identify an activator binding domain (ABD) of ATPase Swi2 and show that this ABD is functionally dispensable, presumably because ABDs of other SWI/SNF subunits can compensate for the loss. In contrast, mutational characterization of the ABD of the Swi2-related ATPase Sth1 revealed that some conserved basic and hydrophobic amino acids within this domain are essential for the function of Sth1. While ABDs of Swi2 and Sth1 define separate functional protein domains, mapping of an ABD within ATPase Ino80 showed co-localization with its HSA domain also required for binding actin-related proteins. Comparative interaction studies finally demonstrated that several unrelated activators each exhibit a specific binding pattern with ABDs of Swi2, Sth1 and Ino80.
Identifiants
pubmed: 39235627
doi: 10.1007/s00294-024-01300-x
pii: 10.1007/s00294-024-01300-x
doi:
Substances chimiques
Saccharomyces cerevisiae Proteins
0
Adenosine Triphosphatases
EC 3.6.1.-
Transcription Factors
0
DNA-Binding Proteins
0
INO80 complex, S cerevisiae
0
Chromosomal Proteins, Non-Histone
0
RSC complex, S cerevisiae
0
STH1 protein, S cerevisiae
EC 3.6.1.-
INO2 protein, S cerevisiae
0
SNF2 protein, S cerevisiae
EC 3.6.1.-
SWI1 protein, S cerevisiae
0
Nuclear Proteins
0
Cell Cycle Proteins
0
Basic Helix-Loop-Helix Transcription Factors
0
Types de publication
Journal Article
Langues
eng
Sous-ensembles de citation
IM
Pagination
15Informations de copyright
© 2024. The Author(s).
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