7PYJ

CryoEM structure of E.coli RNA polymerase elongation complex bound to NusA (NusA elongation complex in less-swiveled conformation)

Summary for 7PYJ

• Entry DOI: 10.2210/pdb7pyj/pdb
• EMDB information: 13717
• Descriptor: DNA-directed RNA polymerase subunit alpha, ZINC ION, DNA-directed RNA polymerase subunit beta, ... (10 entities in total)
• Functional Keywords: nusa, transcription elongation, cryo-em, transcription
• Biological source: Escherichia coli; More
• Total number of polymer chains: 9
• Total formula weight: 473136.50

Authors

Zhu, C.,Guo, X.,Weixlbaumer, A. (deposition date: 2021-10-10, release date: 2022-03-23, Last modification date: 2024-07-17)

Primary citation

Zhu, C.,Guo, X.,Dumas, P.,Takacs, M.,Abdelkareem, M.,Vanden Broeck, A.,Saint-Andre, C.,Papai, G.,Crucifix, C.,Ortiz, J.,Weixlbaumer, A.
Transcription factors modulate RNA polymerase conformational equilibrium.
Nat Commun, 13:1546-1546, 2022

PubMed Abstract: RNA polymerase (RNAP) frequently pauses during the transcription of DNA to RNA to regulate gene expression. Transcription factors NusA and NusG modulate pausing, have opposing roles, but can bind RNAP simultaneously. Here we report cryo-EM reconstructions of Escherichia coli RNAP bound to NusG, or NusA, or both. RNAP conformational changes, referred to as swivelling, correlate with transcriptional pausing. NusA facilitates RNAP swivelling to further increase pausing, while NusG counteracts this role. Their structural effects are consistent with biochemical results on two categories of transcriptional pauses. In addition, the structures suggest a cooperative mechanism of NusA and NusG during Rho-mediated transcription termination. Our results provide a structural rationale for the stochastic nature of pausing and termination and how NusA and NusG can modulate it.

PubMed: 35318334
DOI: 10.1038/s41467-022-29148-0

Experimental method

ELECTRON MICROSCOPY (4.2 Å)