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7Q0K

RNA polymerase elongation complex in less-swiveled conformation

Summary for 7Q0K
Entry DOI10.2210/pdb7q0k/pdb
EMDB information13746
DescriptorntDNA, tDNA, RNA, ... (9 entities in total)
Functional Keywordsrnap transcription elongation, cryo-em, transcription
Biological sourceEscherichia coli
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Total number of polymer chains8
Total formula weight418203.81
Authors
Zhu, C.,Guo, X.,Weixlbaumer, A. (deposition date: 2021-10-15, release date: 2022-03-23, Last modification date: 2024-07-17)
Primary citationZhu, 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
Cited by
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
PDB entries with the same primary citation
Experimental method
ELECTRON MICROSCOPY (4 Å)
Structure validation

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