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Related Concept Videos

Termination of Translation01:44

Termination of Translation

The large ribosomal subunit has several important structures essential to translation. These include the peptidyl transferase center (PTC) - which is the site where the peptide bond is formed - and a large, internal, water-filled tube through which the nascent polypeptide moves. This latter structure is called the Peptide Exit Tunnel, and it begins at the PTC and spans the body of the large ribosomal subunit. During translation, as the nascent polypeptide chain is synthesized, it passes through...
Improving Translational Accuracy02:07

Improving Translational Accuracy

Base complementarity between the three base pairs of mRNA codon and the tRNA anticodon is not a failsafe mechanism. Inaccuracies can range from a single mismatch to no correct base pairing at all. The free energy difference between the correct and nearly correct base pairs can be as small as 3 kcal/ mol. With complementarity being the only proofreading step, the estimated error frequency would be one wrong amino acid in every 100 amino acids incorporated. However, error frequencies observed in...
Initiation of Translation02:33

Initiation of Translation

Initiating translation is complex because it involves multiple molecules. Initiator tRNA, ribosomal subunits, and eukaryotic initiation factors (eIFs) are all required to assemble on the initiation codon of mRNA. This process consists of several steps that are mediated by different eIFs.
First, the initiator tRNA must be selected from the pool of elongator tRNAs by eukaryotic initiation factor 2 (eIF2). The initiator tRNA (Met-tRNAi) has conserved sequence elements including modified bases at...
Initiation of Translation02:33

Initiation of Translation

Initiating translation is complex because it involves multiple molecules. Initiator tRNA, ribosomal subunits, and eukaryotic initiation factors (eIFs) are all required to assemble on the initiation codon of mRNA. This process consists of several steps that are mediated by different eIFs.
First, the initiator tRNA must be selected from the pool of elongator tRNAs by eukaryotic initiation factor 2 (eIF2). The initiator tRNA (Met-tRNAi) has conserved sequence elements including modified bases at...
Cotranslational Protein Translocation01:20

Cotranslational Protein Translocation

Translocation of proteins across membranes is an ancient process that occurs even in bacteria and archaebacteria. In fact, the components of the translocation machinery are still conserved between prokaryotes and eukaryotes.
Sec61 channel partners for cotranslational translocation
During cotranslational translocation, the Sec61 channel partners with the signal recognition particle (SRP), the signal recognition particle receptor (SR), and the ribosomes to transport the nascent polypeptide chain...
Bacterial Protein Maturation01:26

Bacterial Protein Maturation

Bacterial protein maturation is a tightly regulated process that ensures newly synthesized polypeptides achieve correct functional conformations. This maturation involves a series of modifications, folding events, and quality control steps, often assisted by specialized chaperone proteins.N-Terminal ModificationsThe maturation of bacterial polypeptides begins cotranslationally as the polypeptide exits the ribosome. The first amino acid, N-formylmethionine (fMet), is typically modified at the...

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Related Experiment Video

Updated: Jun 18, 2026

Isolation of Ribosome Bound Nascent Polypeptides in vitro to Identify Translational Pause Sites Along mRNA
10:15

Isolation of Ribosome Bound Nascent Polypeptides in vitro to Identify Translational Pause Sites Along mRNA

Published on: July 6, 2012

Structural insight into nascent polypeptide chain-mediated translational stalling.

Birgit Seidelt1, C Axel Innis, Daniel N Wilson

  • 1Gene Center and Center for Integrated Protein Science Munich (CIPSM), Department for Chemistry and Biochemistry, University of Munich, Feodor-Lynen-Strasse 25, 81377 Munich, Germany.

Science (New York, N.Y.)
|November 26, 2009
PubMed
Summary
This summary is machine-generated.

Ribosome stalling during Escherichia coli tryptophanase operon expression is critical. Nascent TnaC peptide interactions within the ribosomal exit tunnel inhibit translation by altering release factor binding sites.

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Using SecM Arrest Sequence as a Tool to Isolate Ribosome Bound Polypeptides
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Using SecM Arrest Sequence as a Tool to Isolate Ribosome Bound Polypeptides

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An In Vitro Single-Molecule Imaging Assay for the Analysis of Cap-Dependent Translation Kinetics
09:52

An In Vitro Single-Molecule Imaging Assay for the Analysis of Cap-Dependent Translation Kinetics

Published on: September 15, 2020

Related Experiment Videos

Last Updated: Jun 18, 2026

Isolation of Ribosome Bound Nascent Polypeptides in vitro to Identify Translational Pause Sites Along mRNA
10:15

Isolation of Ribosome Bound Nascent Polypeptides in vitro to Identify Translational Pause Sites Along mRNA

Published on: July 6, 2012

Using SecM Arrest Sequence as a Tool to Isolate Ribosome Bound Polypeptides
09:42

Using SecM Arrest Sequence as a Tool to Isolate Ribosome Bound Polypeptides

Published on: June 19, 2012

An In Vitro Single-Molecule Imaging Assay for the Analysis of Cap-Dependent Translation Kinetics
09:52

An In Vitro Single-Molecule Imaging Assay for the Analysis of Cap-Dependent Translation Kinetics

Published on: September 15, 2020

Area of Science:

  • Molecular Biology
  • Structural Biology
  • Microbiology

Background:

  • Gene expression regulation in bacteria is crucial for cellular function.
  • The Escherichia coli tryptophanase operon's expression is controlled by translation of the TnaC leader peptide.
  • Ribosome stalling during TnaC translation is a key regulatory mechanism.

Purpose of the Study:

  • To elucidate the structural basis of ribosome stalling during TnaC leader peptide translation.
  • To understand how nascent chain interactions within the ribosomal exit tunnel regulate translation.
  • To investigate the mechanism by which stalling inhibits translation.

Main Methods:

  • Cryo-electron microscopy (cryo-EM) at 5.8 angstrom resolution.
  • Single-particle reconstruction of stalled ribosomes.
  • Structural analysis of nascent chain-ribosome interactions.

Main Results:

  • Determined the structure of a ribosome stalled during tnaC leader gene translation.
  • Identified specific contacts between the TnaC nascent chain and the ribosomal exit tunnel.
  • Observed conformational changes in the peptidyltransferase center that prevent release factor binding.
  • Demonstrated that nascent chains adopt distinct conformations within the ribosomal exit tunnel.

Conclusions:

  • Nascent chain interactions within the ribosomal exit tunnel are critical for regulating translation.
  • A model is proposed where tunnel interactions signal to the peptidyltransferase center to inhibit translation.
  • Nascent chain conformation within the ribosome is dynamic and plays a regulatory role.