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Videos de Conceptos Relacionados

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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Video Experimental Relacionado

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

Conocimiento estructural sobre el estancamiento traslacional mediado por la cadena polipeptídica naciente.

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
Resumen

El estancamiento del ribosoma durante la expresión del operón de la triptofanasa de Escherichia coli es crítico. Las interacciones del péptido TnaC nacientes dentro del túnel de salida ribosomal inhiben la traducción al alterar los sitios de unión del factor de liberación.

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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

Published on: June 19, 2012

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

Published on: September 15, 2020

Videos de Experimentos Relacionados

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

Área de la Ciencia:

  • Biología Molecular Biología Molecular
  • Biología Estructural Biología estructural.
  • Microbiología Microbiología.

Sus antecedentes:

  • La regulación de la expresión génica en las bacterias es crucial para la función celular.
  • La expresión del operón triptofanasa de Escherichia coli está controlada por la traducción del péptido líder TnaC.
  • El estancamiento de los ribosomas durante la traducción de TnaC es un mecanismo regulador clave.

Objetivo del estudio:

  • Para dilucidar las bases estructurales del estancamiento del ribosoma durante la traducción del péptido líder TnaC.
  • Comprender cómo las interacciones de la cadena naciente dentro del túnel de salida ribosomal regulan la traducción.
  • Investigar el mecanismo por el cual el estancamiento inhibe la traducción.

Principales métodos:

  • Microscopía cryoelectrónica (cryo-EM) con una resolución de 5,8 angstroms.
  • Reconstrucción de una sola partícula de los ribosomas estancados.
  • Análisis estructural de las interacciones cadena-ribosoma nacientes.

Principales resultados:

  • Determinó la estructura de un ribosoma estancado durante la traducción del gen líder tnaC.
  • Se identificaron contactos específicos entre la cadena naciente de TnaC y el túnel de salida ribosomal.
  • Cambios conformacionales observados en el centro de la peptidiltransferasa que impiden la unión del factor de liberación.
  • Se demostró que las cadenas nacientes adoptan conformaciones distintas dentro del túnel de salida ribosomal.

Conclusiones:

  • Las interacciones en cadena nacientes dentro del túnel de salida ribosomal son críticas para regular la traducción.
  • Se propone un modelo donde las interacciones de túnel señalan al centro de la peptidiltransferasa para inhibir la traducción.
  • La conformación de la cadena naciente dentro del ribosoma es dinámica y juega un papel regulador.