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Cited by 32RNA and protein synthesis mechanismsBacterial Genetics and BiotechnologyRNA modifications and cancer

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Molecular basis of mRNA delivery to the bacterial ribosome

Open access
Webster, Michael W., Chauvier, Adrien, Rahil, Huma, Graziadei, Andrea, Charles, Kristine, Miropolskaya, Nataliya, Takacs, Maria, Saint-André, Charlotte, Rappsilber, Juri, Walter, Nils G., Weixlbaumer, Albert·2024·Science
DOI 10.1126/science.ado8476PMC PMC13040446

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Abstract

Protein synthesis begins with the formation of a ribosome-messenger RNA (mRNA) complex. In bacteria, the small ribosomal subunit (30 S ) 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 S . Here, we examined 30 S 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 S 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 S recruitment to mRNAs and establish transcription-translation coupling.

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Metadata

Authors
Webster, M. W., Chauvier, A., Rahil, H., Graziadei, A., Charles, K., Miropolskaya, N., Takacs, M., Saint-André, C., Rappsilber, J., Walter, N. G., & Weixlbaumer, A.
Affiliations
  • John Innes Centre (GB)
  • University of Michigan (US)
  • Centre National de la Recherche Scientifique (FR)
  • Technische Universität Berlin (DE)
  • Department of Integrated Structural Biology, Institut de Génétique et de Biologie Moléculaire et Cellulaire (IGBMC), Illkirch Cedex, France.
  • Wellcome Centre for Cell Biology (GB)
Corresponding author
  • Webster, Michael W.
  • Chauvier, Adrien
  • Rahil, Huma
  • Graziadei, Andrea
  • Weixlbaumer, Albert
ORCID
Venue
Science
Publisher
American Association for the Advancement of Science (AAAS)
Published
2024-11-29
Volume
386
Issue
6725
Pages
eado8476-eado8476
ISSN
  • 0036-8075 (ISSN-L)
  • 1095-9203
DOI
10.1126/science.ado8476
PMC
PMC13040446
OpenAlex
W4404810290
Cited by
32
References
2
Citations by year
2026: 15 · 2025: 15 · 2024: 2
FWCI
4.36
Type
journal article
Language
en
Open access
Licence
cc-by
Locations
  • Science (publishedVersion, cc-by)
  • bioRxiv (Cold Spring Harbor Laboratory) (acceptedVersion, cc-by-nc-nd)
  • PubMed (publishedVersion)
  • PubMed Central (publishedVersion)
  • PubMed Central (submittedVersion, cc-by-nc-nd)
  • HAL (submittedVersion, other-oa)
Funders
  • Wellcome Trust (203149, ANR-10-LABX-0030-INRT)
  • Agence Nationale de la Recherche (ANR-10-IDEX-0002, ANR-10- INBS-05, ANR-10-IDEX, ANR-10-LABX-0030, ANR-10-IDEX0002-02, ANR-10, ANR-10-INBS-0005)
  • French Infrastructure for Integrated Structural Biology (ANR‐10‐LABX‐0030‐INRT, ANR-10-INBS-0.5, ANR-10-IDEX-0002-02)
  • National Institutes of Health (ANR-10-LABX-0030-INRT)
  • Biotechnology and Biological Sciences Research Council (BBP0135111, BB/P013511, 203149, BB/X01102X/1, BBS/E/JI/230002B, BB/X01102X)
  • National Institute of General Medical Sciences (R35GM131922)
Topics
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › RNA and protein synthesis mechanisms
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Genetics › Bacterial Genetics and Biotechnology
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › RNA modifications and cancer
Keywords
Shine-Dalgarno sequence, ribosomal protein S1, RNA polymerase, translation initiation, transcription-translation coupling, nascent mRNA, base pairing, ribosome-mRNA complex

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