7XUE

Cryo-EM structure of HK022 putRNA-associated E.coli RNA polymerase elongation complex

Summary for 7XUE

• Entry DOI: 10.2210/pdb7xue/pdb
• EMDB information: 33466
• Descriptor: non-template DNA, template DNA, RNA (nun gene and immunity region), ... (9 entities in total)
• Functional Keywords: transcription, rna polymerase, anti-pausing, anti-termination, cryo-em, hk022 put
• Biological source: Escherichia coli (strain K12); More
• Total number of polymer chains: 8
• Total formula weight: 532400.55

Authors

Hwang, S.H.,Kang, J.Y. (deposition date: 2022-05-18, release date: 2022-08-10, Last modification date: 2024-07-03)

Primary citation

Hwang, S.,Olinares, P.D.B.,Lee, J.,Kim, J.,Chait, B.T.,King, R.A.,Kang, J.Y.
Structural basis of transcriptional regulation by a nascent RNA element, HK022 putRNA.
Nat Commun, 13:4668-4668, 2022

PubMed Abstract: Transcription, in which RNA polymerases (RNAPs) produce RNA from DNA, is the first step of gene expression. As such, it is highly regulated either by trans-elements like protein factors and/or by cis-elements like specific sequences on the DNA. Lambdoid phage HK022 contains a cis-element, put, which suppresses pausing and termination during transcription of the early phage genes. The putRNA transcript solely performs the anti-pausing/termination activities by interacting directly with the E.coli RNAP elongation complex (EC) by an unknown structural mechanism. In this study, we reconstituted putRNA-associated ECs and determined the structures using cryo-electron microscopy. The determined structures of putRNA-associated EC, putRNA-absent EC, and σ-bound EC suggest that the putRNA interaction with the EC counteracts swiveling, a conformational change previously identified to promote pausing and σ might modulate putRNA folding via σ-dependent pausing during elongation.

PubMed: 35970830
DOI: 10.1038/s41467-022-32315-y

Experimental method

ELECTRON MICROSCOPY (3.17 Å)