6xdq
From Proteopedia
Cryo-EM structure of an Escherichia coli coupled transcription-translation complex B3 (TTC-B3) containing an mRNA with a 30 nt long spacer, transcription factors NusA and NusG, and fMet-tRNAs at P-site and E-site
Structural highlights
FunctionRL11_ECOLI This protein binds directly to 23S ribosomal RNA. Forms the L11 stalk, which is mobile in the ribosome, indicating its contribution to the activity of initiation, elongation and release factors.[HAMAP-Rule:MF_00736_B] Publication Abstract from PubMedIn bacteria, transcription and translation are coupled processes in which the movement of RNA polymerase (RNAP)-synthesizing messenger RNA (mRNA) is coordinated with the movement of the first ribosome-translating mRNA. Coupling is modulated by the transcription factors NusG (which is thought to bridge RNAP and the ribosome) and NusA. Here, we report cryo-electron microscopy structures of Escherichia coli transcription-translation complexes (TTCs) containing different-length mRNA spacers between RNAP and the ribosome active-center P site. Structures of TTCs containing short spacers show a state incompatible with NusG bridging and NusA binding (TTC-A, previously termed "expressome"). Structures of TTCs containing longer spacers reveal a new state compatible with NusG bridging and NusA binding (TTC-B) and reveal how NusG bridges and NusA binds. We propose that TTC-B mediates NusG- and NusA-dependent transcription-translation coupling. Structural basis of transcription-translation coupling.,Wang C, Molodtsov V, Firlar E, Kaelber JT, Blaha G, Su M, Ebright RH Science. 2020 Sep 11;369(6509):1359-1365. doi: 10.1126/science.abb5317. Epub 2020, Aug 20. PMID:32820061[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. Loading citation details.. Citations No citations found See AlsoReferences
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