Structural basis for TBP displacement from TATA box DNA by the Swi2/Snf2 ATPase Mot1.
Journal
Nature structural & molecular biology
ISSN: 1545-9985
Titre abrégé: Nat Struct Mol Biol
Pays: United States
ID NLM: 101186374
Informations de publication
Date de publication:
05 2023
05 2023
Historique:
received:
22
03
2022
accepted:
13
03
2023
medline:
19
5
2023
pubmed:
28
4
2023
entrez:
27
4
2023
Statut:
ppublish
Résumé
The Swi2/Snf2 family transcription regulator Modifier of Transcription 1 (Mot1) uses adenosine triphosphate (ATP) to dissociate and reallocate the TATA box-binding protein (TBP) from and between promoters. To reveal how Mot1 removes TBP from TATA box DNA, we determined cryogenic electron microscopy structures that capture different states of the remodeling reaction. The resulting molecular video reveals how Mot1 dissociates TBP in a process that, intriguingly, does not require DNA groove tracking. Instead, the motor grips DNA in the presence of ATP and swings back after ATP hydrolysis, moving TBP to a thermodynamically less stable position on DNA. Dislodged TBP is trapped by a chaperone element that blocks TBP's DNA binding site. Our results show how Swi2/Snf2 proteins can remodel protein-DNA complexes through DNA bending without processive DNA tracking and reveal mechanistic similarities to RNA gripping DEAD box helicases and RIG-I-like immune sensors.
Identifiants
pubmed: 37106137
doi: 10.1038/s41594-023-00966-0
pii: 10.1038/s41594-023-00966-0
doi:
Substances chimiques
Adenosine Triphosphatases
EC 3.6.1.-
Transcription Factors
0
TATA-Box Binding Protein
0
Saccharomyces cerevisiae Proteins
0
DNA
9007-49-2
Adenosine Triphosphate
8L70Q75FXE
TATA-Binding Protein Associated Factors
0
Types de publication
Journal Article
Research Support, Non-U.S. Gov't
Langues
eng
Sous-ensembles de citation
IM
Pagination
640-649Informations de copyright
© 2023. The Author(s), under exclusive licence to Springer Nature America, Inc.
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