Loading
PDBj
MenuPDBj@FacebookPDBj@X(formerly Twitter)PDBj@BlueSkyPDBj@YouTubewwPDB FoundationwwPDBDonate
RCSB PDBPDBeBMRBAdv. SearchSearch help

8RAO

Structure of Sen1-ADP.BeF3-RNA complex

Summary for 8RAO
Entry DOI10.2210/pdb8rao/pdb
EMDB information19021
DescriptorHelicase SEN1, RNA, ADENOSINE-5'-DIPHOSPHATE, ... (5 entities in total)
Functional Keywordsrna polymerase ii, pol ii, termination, sen1, gene regulation
Biological sourceSaccharomyces cerevisiae (brewer's yeast)
More
Total number of polymer chains2
Total formula weight264636.22
Authors
Rengachari, S.,Lidscreiber, M.,Cramer, P. (deposition date: 2023-12-01, release date: 2024-10-30, Last modification date: 2025-02-26)
Primary citationRengachari, S.,Hainthaler, T.,Oberthuer, C.,Lidschreiber, M.,Cramer, P.
Mechanism of polyadenylation-independent RNA polymerase II termination.
Nat.Struct.Mol.Biol., 32:339-345, 2025
Cited by
PubMed Abstract: The mechanisms underlying the initiation and elongation of RNA polymerase II (Pol II) transcription are well-studied, whereas termination remains poorly understood. Here we analyze the mechanism of polyadenylation-independent Pol II termination mediated by the yeast Sen1 helicase. Cryo-electron microscopy structures of two pretermination intermediates show that Sen1 binds to Pol II and uses its adenosine triphosphatase activity to pull on exiting RNA in the 5' direction. This is predicted to push Pol II forward, induce an unstable hypertranslocated state and destabilize the transcription bubble, thereby facilitating termination. This mechanism of transcription termination may be widely used because it is conceptually conserved in the bacterial transcription system.
PubMed: 39424994
DOI: 10.1038/s41594-024-01409-0
PDB entries with the same primary citation
Experimental method
ELECTRON MICROSCOPY (4.4 Å)
Structure validation

236371

PDB entries from 2025-05-21

PDB statisticsPDBj update infoContact PDBjnumon