Molecular basis of mRNA delivery to the bacterial ribosome

Protein synthesis begins with the formation of a ribosome-messenger RNA (mRNA) complex. In bacteria, the small ribosomal subunit (30<i>S</i>) is recruited to many mRNAs through base pairing with the Shine-Dalgarno (SD) sequence and RNA binding by ribosomal protein bS1. Translation can initiate on nascent mRNAs, and RNA polymerase (RNAP) can promote the recruitment of the pioneering 30<i>S</i>. Here, we examined 30<i>S</i> recruitment to nascent mRNAs using cryo-electron microscopy, single-molecule fluorescence colocalization, and in-cell cross-linking mass spectrometry. We show that bS1 delivers the mRNA to the ribosome for SD duplex formation and 30<i>S</i> activation. Additionally, bS1 and RNAP stimulate translation initiation. Our work provides a mechanistic framework for how the SD duplex, ribosomal proteins, and RNAP cooperate in 30<i>S</i> recruitment to mRNAs and establish transcription-translation coupling.

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Publication Details

Journal
Science
Published
2024-11-28
DOI
https://doi.org/10.1126/science.ado8476
Citations
21
Primary Topic
RNA and protein synthesis mechanisms
Type
article
Field-Weighted Citation Impact
4.91

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article

Molecular basis of mRNA delivery to the bacterial ribosome

Nataliya Miropolskaya, Andrea Graziadei, Nils G. Walter, Huma Rahil et al.
21 citations
Science
RNA and protein synthesis mechanisms
4.91
article

Molecular basis of mRNA delivery to the bacterial ribosome

Nataliya Miropolskaya, Andrea Graziadei, Nils G. Walter, Huma Rahil, Kristine Charles, Adrien Chauvier, Michael Webster, Charlotte Saint-André, Albert Weixlbaumer, Juri Rappsilber, Mária Takács
article en
21 citations

Abstract

Protein synthesis begins with the formation of a ribosome-messenger RNA (mRNA) complex. In bacteria, the small ribosomal subunit (30<i>S</i>) is recruited to many mRNAs through base pairing with the Shine-Dalgarno (SD) sequence and RNA binding by ribosomal protein bS1. Translation can initiate on nascent mRNAs, and RNA polymerase (RNAP) can promote the recruitment of the pioneering 30<i>S</i>. Here, we examined 30<i>S</i> recruitment to nascent mRNAs using cryo-electron microscopy, single-molecule fluorescence colocalization, and in-cell cross-linking mass spectrometry. We show that bS1 delivers the mRNA to the ribosome for SD duplex formation and 30<i>S</i> activation. Additionally, bS1 and RNAP stimulate translation initiation. Our work provides a mechanistic framework for how the SD duplex, ribosomal proteins, and RNAP cooperate in 30<i>S</i> recruitment to mRNAs and establish transcription-translation coupling.

ScienceVol. 386(6725)
John Innes Centre (GB), Centre National de la Recherche Scientifique (FR), Inserm (FR), University of Michigan (US), Norwich Research Park (GB), Institut de génétique et de biologie moléculaire et cellulaire (FR), Wellcome Centre for Cell Biology (GB), Technische Universität Berlin (DE), Université de Strasbourg (FR), Analysis Group (United States) (US)
Biotechnology and Biological Sciences Research Council
Openalex Percentile: Top 4%
RNA and protein synthesis mechanisms
4.91
DOIOpen Access PDFOpenAlex
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