9BCU

Cryo-EM structure of Thermococcus kodakarensis FttA-dependent transcription pre-termination complex containing 52 nt RNA

Summary for 9BCU

• Entry DOI: 10.2210/pdb9bcu/pdb
• EMDB information: 44439
• Descriptor: DNA-directed RNA polymerase subunit A', DNA-directed RNA polymerase subunit N, DNA-directed RNA polymerase subunit P, ... (19 entities in total)
• Functional Keywords: rna polymerase, pre-termination complex, ftta, archaea, transcription
• Biological source: Thermococcus kodakarensis; More
• Total number of polymer chains: 18
• Total formula weight: 591602.74

Authors

You, L.,Ebright, R.H. (deposition date: 2024-04-09, release date: 2024-07-31, Last modification date: 2024-11-13)

Primary citation

You, L.,Wang, C.,Molodtsov, V.,Kuznedelov, K.,Miao, X.,Wenck, B.R.,Ulisse, P.,Sanders, T.J.,Marshall, C.J.,Firlar, E.,Kaelber, J.T.,Santangelo, T.J.,Ebright, R.H.
Structural basis of archaeal FttA-dependent transcription termination.
Nature, 635:229-236, 2024

PubMed Abstract: The ribonuclease FttA (also known as aCPSF and aCPSF1) mediates factor-dependent transcription termination in archaea. Here we report the structure of a Thermococcus kodakarensis transcription pre-termination complex comprising FttA, Spt4, Spt5 and a transcription elongation complex (TEC). The structure shows that FttA interacts with the TEC in a manner that enables RNA to proceed directly from the TEC RNA-exit channel to the FttA catalytic centre and that enables endonucleolytic cleavage of RNA by FttA, followed by 5'→3' exonucleolytic cleavage of RNA by FttA and concomitant 5'→3' translocation of FttA on RNA, to apply mechanical force to the TEC and trigger termination. The structure further reveals that Spt5 bridges FttA and the TEC, explaining how Spt5 stimulates FttA-dependent termination. The results reveal functional analogy between bacterial and archaeal factor-dependent termination, functional homology between archaeal and eukaryotic factor-dependent termination, and fundamental mechanistic similarities in factor-dependent termination in bacteria, archaea, and eukaryotes.

PubMed: 39322680
DOI: 10.1038/s41586-024-07979-9

Experimental method

ELECTRON MICROSCOPY (2.2 Å)