Structure of the transcribing RNA polymerase II-Elongin complex.
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:
Dec 2023
Dec 2023
Historique:
received:
02
03
2023
accepted:
26
09
2023
pubmed:
7
11
2023
medline:
7
11
2023
entrez:
6
11
2023
Statut:
ppublish
Résumé
Elongin is a heterotrimeric elongation factor for RNA polymerase (Pol) II transcription that is conserved among metazoa. Here, we report three cryo-EM structures of human Elongin bound to transcribing Pol II. The structures show that Elongin subunit ELOA binds the RPB2 side of Pol II and anchors the ELOB-ELOC subunit heterodimer. ELOA contains a 'latch' that binds between the end of the Pol II bridge helix and funnel helices, thereby inducing a conformational change near the polymerase active center. The latch is required for the elongation-stimulatory activity of Elongin, but not for Pol II binding, indicating that Elongin functions by allosterically regulating the conformational mobility of the polymerase active center. Elongin binding to Pol II is incompatible with association of the super elongation complex, PAF1 complex and RTF1, which also contain an elongation-stimulatory latch element.
Identifiants
pubmed: 37932450
doi: 10.1038/s41594-023-01138-w
pii: 10.1038/s41594-023-01138-w
doi:
Types de publication
Journal Article
Langues
eng
Sous-ensembles de citation
IM
Pagination
1925-1935Informations de copyright
© 2023. The Author(s).
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