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From Proteopedia
E. coli 70S-RNAP expressome complex in collided state bound to NusG
Structural highlights
FunctionRS9_ECOLI The C-terminal tail plays a role in the affinity of the 30S P site for different tRNAs. Mutations that decrease this affinity are suppressed in the 70S ribosome.[1] Publication Abstract from PubMedProkaryotic messenger RNAs (mRNAs) are translated as they are transcribed. The lead ribosome potentially contacts RNA polymerase (RNAP) and forms a supramolecular complex known as the expressome. The basis of expressome assembly and its consequences for transcription and translation are poorly understood. Here, we present a series of structures representing uncoupled, coupled, and collided expressome states determined by cryo-electron microscopy. A bridge between the ribosome and RNAP can be formed by the transcription factor NusG, which stabilizes an otherwise-variable interaction interface. Shortening of the intervening mRNA causes a substantial rearrangement that aligns the ribosome entrance channel to the RNAP exit channel. In this collided complex, NusG linkage is no longer possible. These structures reveal mechanisms of coordination between transcription and translation and provide a framework for future study. Structural basis of transcription-translation coupling and collision in bacteria.,Webster MW, Takacs M, Zhu C, Vidmar V, Eduljee A, Abdelkareem M, Weixlbaumer A Science. 2020 Sep 11;369(6509):1355-1359. doi: 10.1126/science.abb5036. Epub 2020, Aug 20. PMID:32820062[2] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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