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8YFQ

Cryo EM structure of Komagataella phaffii RNAPII-Rat1-Rai1 pre-termination complex

Summary for 8YFQ
Entry DOI10.2210/pdb8yfq/pdb
Related8YF5 8YFE 8YFR
EMDB information39211 39221 39226 39227
DescriptorDNA-directed RNA polymerase subunit, RNA polymerase subunit ABC10-beta, common to RNA polymerases I, II, and III, RNA polymerase II subunit B12.5, ... (19 entities in total)
Functional Keywordstranscription termination, rna polymerase ii, transcription
Biological sourceKomagataella phaffii
More
Total number of polymer chains17
Total formula weight733453.19
Authors
Murayama, Y.,Yanagisawa, T.,Ehara, H.,Sekine, S. (deposition date: 2024-02-25, release date: 2024-09-25)
Primary citationYanagisawa, T.,Murayama, Y.,Ehara, H.,Goto, M.,Aoki, M.,Sekine, S.I.
Structural basis of eukaryotic transcription termination by the Rat1 exonuclease complex.
Nat Commun, 15:7854-7854, 2024
Cited by
PubMed Abstract: The 5´-3´ exoribonuclease Rat1/Xrn2 is responsible for the termination of eukaryotic mRNA transcription by RNAPII. Rat1 forms a complex with its partner proteins, Rai1 and Rtt103, and acts as a "torpedo" to bind transcribing RNAPII and dissociate DNA/RNA from it. Here we report the cryo-electron microscopy structures of the Rat1-Rai1-Rtt103 complex and three Rat1-Rai1-associated RNAPII complexes (type-1, type-1b, and type-2) from the yeast, Komagataella phaffii. The Rat1-Rai1-Rtt103 structure revealed that Rat1 and Rai1 form a heterotetramer with a single Rtt103 bound between two Rai1 molecules. In the type-1 complex, Rat1-Rai1 forms a heterodimer and binds to the RNA exit site of RNAPII to extract RNA into the Rat1 exonuclease active site. This interaction changes the RNA path in favor of termination (the "pre-termination" state). The type-1b and type-2 complexes have no bound DNA/RNA, likely representing the "post-termination" states. These structures illustrate the termination mechanism of eukaryotic mRNA transcription.
PubMed: 39245712
DOI: 10.1038/s41467-024-52157-0
PDB entries with the same primary citation
Experimental method
ELECTRON MICROSCOPY (3.3 Å)
Structure validation

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