7py0
CryoEM structure of E.coli RNA polymerase elongation complex bound to NusG (NusG-EC in more-swiveled conformation)CryoEM structure of E.coli RNA polymerase elongation complex bound to NusG (NusG-EC in more-swiveled conformation)
Structural highlights
FunctionRPOZ_ECOLI Promotes RNA polymerase assembly. Latches the N- and C-terminal regions of the beta' subunit thereby facilitating its interaction with the beta and alpha subunits.[HAMAP-Rule:MF_00366] 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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