Structural highlights
Function
RL15_ECOLI This protein binds the 5S rRNA. It is required for the late stages of subunit assembly, and is essential for 5S rRNA assembly onto the ribosome.[HAMAP-Rule:MF_01341_B]
Publication Abstract from PubMed
In 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.
See Also
References
- ↑ Wang C, Molodtsov V, Firlar E, Kaelber JT, Blaha G, Su M, Ebright RH. Structural basis of transcription-translation coupling. Science. 2020 Sep 11;369(6509):1359-1365. PMID:32820061 doi:10.1126/science.abb5317
