Structures of co-transcriptional RNA capping enzymes on paused transcription complex.
Journal
Nature communications
ISSN: 2041-1723
Titre abrégé: Nat Commun
Pays: England
ID NLM: 101528555
Informations de publication
Date de publication:
30 May 2024
30 May 2024
Historique:
received:
09
08
2023
accepted:
17
05
2024
medline:
31
5
2024
pubmed:
31
5
2024
entrez:
30
5
2024
Statut:
epublish
Résumé
The 5'-end capping of nascent pre-mRNA represents the initial step in RNA processing, with evidence demonstrating that guanosine addition and 2'-O-ribose methylation occur in tandem with early steps of transcription by RNA polymerase II, especially at the pausing stage. Here, we determine the cryo-EM structures of the paused elongation complex in complex with RNGTT, as well as the paused elongation complex in complex with RNGTT and CMTR1. Our findings show the simultaneous presence of RNGTT and the NELF complex bound to RNA polymerase II. The NELF complex exhibits two conformations, one of which shows a notable rearrangement of NELF-A/D compared to that of the paused elongation complex. Moreover, CMTR1 aligns adjacent to RNGTT on the RNA polymerase II stalk. Our structures indicate that RNGTT and CMTR1 directly bind the paused elongation complex, illuminating the mechanism by which 5'-end capping of pre-mRNA during transcriptional pausing.
Identifiants
pubmed: 38816438
doi: 10.1038/s41467-024-48963-1
pii: 10.1038/s41467-024-48963-1
doi:
Substances chimiques
RNA Polymerase II
EC 2.7.7.-
RNA Caps
0
RNA Precursors
0
RNA, Messenger
0
Saccharomyces cerevisiae Proteins
0
Types de publication
Journal Article
Langues
eng
Sous-ensembles de citation
IM
Pagination
4622Subventions
Organisme : National Natural Science Foundation of China (National Science Foundation of China)
ID : 31630002,32371251
Informations de copyright
© 2024. The Author(s).
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