7py7
CryoEM structure of E.coli RNA polymerase elongation complex bound to NusA and NusG (NusA and NusG elongation complex in more-swiveled conformation)CryoEM structure of E.coli RNA polymerase elongation complex bound to NusA and NusG (NusA and NusG elongation complex in more-swiveled conformation)
Structural highlights
FunctionRPOA_ECOLI DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates. This subunit plays an important role in subunit assembly since its dimerization is the first step in the sequential assembly of subunits to form the holoenzyme.[HAMAP-Rule:MF_00059] Publication Abstract from PubMedRNA 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. Transcription factors modulate RNA polymerase conformational equilibrium.,Zhu C, Guo X, Dumas P, Takacs M, Abdelkareem M, Vanden Broeck A, Saint-Andre C, Papai G, Crucifix C, Ortiz J, Weixlbaumer A Nat Commun. 2022 Mar 22;13(1):1546. doi: 10.1038/s41467-022-29148-0. PMID:35318334[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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