Structural basis of transcription-translation coupling and collision in bacteria

Prokaryotic 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 under...

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Bibliographic Details
Published in:Science (American Association for the Advancement of Science) 2020-09, Vol.369 (6509), p.1355-1359
Main Authors: Webster, Michael William, Takacs, Maria, Zhu, Chengjin, Vidmar, Vita, Eduljee, Ayesha, Abdelkareem, Mo'men, Weixlbaumer, Albert
Format: Article
Language:English
Subjects:
Bacteria
Biochemistry, Molecular Biology
Contact potentials
Coupling
Cryoelectron Microscopy
DNA-Directed RNA Polymerases - chemistry
Electron microscopy
Elongated structure
Entrances
Escherichia coli - genetics
Escherichia coli Proteins - chemistry
Gene Expression Regulation, Bacterial
Life Sciences
Microscopy
Peptide Elongation Factors - chemistry
Protein Binding
Protein Biosynthesis
Protein Conformation
Ribosome Subunits, Large, Bacterial - chemistry
RNA polymerase
RNA, Messenger - chemistry
Transcription
Transcription Factors - chemistry
Transcription, Genetic
Translation
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Summary:Prokaryotic 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.
ISSN:0036-8075
1095-9203
DOI:10.1126/science.abb5036