9GR1

E. coli 70S-TEC complex in delivery state

This is a non-PDB format compatible entry.

Summary for 9GR1

• Entry DOI: 10.2210/pdb9gr1/pdb
• EMDB information: 51517
• Descriptor: 50S ribosomal protein L33, Small ribosomal subunit protein bS6, fully modified isoform, Small ribosomal subunit protein uS7, ... (59 entities in total)
• Functional Keywords: ribosome, rna polymerase, mrna, gene regulation
• Biological source: Escherichia coli; More
• Total number of polymer chains: 55
• Total formula weight: 2212567.36

Authors

Webster, M.W.,Weixlbaumer, A. (deposition date: 2024-09-10, release date: 2024-11-20, Last modification date: 2025-03-12)

Primary citation

Webster, M.W.,Chauvier, A.,Rahil, H.,Graziadei, A.,Charles, K.,Miropolskaya, N.,Takacs, M.,Saint-Andre, C.,Rappsilber, J.,Walter, N.G.,Weixlbaumer, A.
Molecular basis of mRNA delivery to the bacterial ribosome.
Science, 386:eado8476-eado8476, 2024

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

PubMed: 39607923
DOI: 10.1126/science.ado8476

Experimental method

ELECTRON MICROSCOPY (3.17 Å)