Jove
Visualize
Contáctanos
JoVE
x logofacebook logolinkedin logoyoutube logo
ACERCA DE JoVE
Visión GeneralLiderazgoBlogCentro de Ayuda JoVE
AUTORES
Proceso de PublicaciónConsejo EditorialAlcance y PolíticasRevisión por ParesPreguntas FrecuentesEnviar
BIBLIOTECARIOS
TestimoniosSuscripcionesAccesoRecursosConsejo Asesor de BibliotecasPreguntas Frecuentes
INVESTIGACIÓN
JoVE JournalMethods CollectionsJoVE Encyclopedia of ExperimentsArchivo
EDUCACIÓN
JoVE CoreJoVE BusinessJoVE Science EducationJoVE Lab ManualCentro de Recursos para ProfesoresSitio de Profesores
Términos y Condiciones de Uso
Política de Privacidad
Políticas

Videos de Conceptos Relacionados

Initiation of Translation02:33

Initiation of Translation

40.1K
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...
40.1K
Initiation of Translation02:33

Initiation of Translation

8.5K
8.5K
Improving Translational Accuracy02:07

Improving Translational Accuracy

15.4K
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...
15.4K
Translation in Prokaryotes01:29

Translation in Prokaryotes

2.4K
Prokaryote translation is a complex, highly coordinated process that converts genetic information from mRNA into functional proteins. It involves three stages: initiation, elongation, and termination, each facilitated by specific molecular components.Initiation of TranslationThe process begins with the assembly of the ribosomal subunits and initiation factors on the mRNA. In bacteria, the 30S ribosomal subunit recognizes the Shine-Dalgarno sequence in the mRNA, a conserved region upstream of...
2.4K
Termination of Translation01:44

Termination of Translation

28.5K
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...
28.5K
Ribosomal RNA Synthesis02:53

Ribosomal RNA Synthesis

15.1K
Ribosome synthesis is a highly complex and coordinated process involving more than 200 assembly factors. The synthesis and processing of ribosomal components occurs not only in the nucleolus but also in the nucleoplasm and the cytoplasm of eukaryotic cells.
Ribosome biogenesis begins with the synthesis of 5S and 45S pre-rRNAs by distinct RNA polymerases. The primary transcripts are extensively processed and modified before they are bound and folded by ribosomal proteins and assembly factors,...
15.1K

También podría leer

Artículos Relacionados

Artículos vinculados a este trabajo por autores compartidos, revista y gráfico de citas.

Ordenar por
Same author

Solution structure of mouse HBS1L/SKI7-specific UBA domain in complex with ubiquitin: Implications for stalled ribosome recognition.

PloS one·2026
Same author

The interferon-stimulated gene product HERC5 inhibits human LINE-1 retrotransposition with an ISGylation-independent mechanism.

Nucleic acids research·2026
Same author

Clinical characteristics and prognosis of patients with acute exacerbations of idiopathic interstitial pneumonia: factor and cluster analyses.

Scientific reports·2026
Same author

Secondary Aplastic Anemia During Osimertinib Treatment for Lung Adenocarcinoma: A Case Report.

The Tokai journal of experimental and clinical medicine·2026
Same author

Comprehensive understanding of the correlation between structure and harmonic properties of multicore superparamagnetic particles.

Nanoscale·2026
Same author

Pathogenicity of the novel antigenic variant infectious bursal disease virus B2977CE2C3 isolated in Japan: Histological analysis of experimentally infected chickens.

Veterinary pathology·2026

Video Experimental Relacionado

Updated: Mar 25, 2026

Monitoring eIF4F Assembly by Measuring eIF4E-eIF4G Interaction in Live Cells
08:47

Monitoring eIF4F Assembly by Measuring eIF4E-eIF4G Interaction in Live Cells

Published on: May 1, 2020

3.4K

Estructura cristalina del factor de iniciación de la traducción eucariota 2B

Kazuhiro Kashiwagi1,2,3, Mari Takahashi3, Madoka Nishimoto3

  • 1Graduate School of Science, The University of Tokyo, Bunkyo-ku, Tokyo 113-0033, Japan.

Nature
|February 23, 2016
PubMed
Resumen

Los científicos determinaron la estructura del factor de iniciación de la traducción eucariota 2B (eIF2B), revelando cómo la fosforilación inducida por el estrés de eIF2α crea un complejo no productivo, que inhibe la síntesis de proteínas. Esto proporciona una visión de las respuestas de estrés celular.

Más Videos Relacionados

Rapid In Vivo Fixation and Isolation of Translational Complexes from Eukaryotic Cells
14:29

Rapid In Vivo Fixation and Isolation of Translational Complexes from Eukaryotic Cells

Published on: December 25, 2021

4.9K
Toeprinting Analysis of Translation Initiation Complex Formation on Mammalian mRNAs
10:37

Toeprinting Analysis of Translation Initiation Complex Formation on Mammalian mRNAs

Published on: May 10, 2018

13.3K

Videos de Experimentos Relacionados

Last Updated: Mar 25, 2026

Monitoring eIF4F Assembly by Measuring eIF4E-eIF4G Interaction in Live Cells
08:47

Monitoring eIF4F Assembly by Measuring eIF4E-eIF4G Interaction in Live Cells

Published on: May 1, 2020

3.4K
Rapid In Vivo Fixation and Isolation of Translational Complexes from Eukaryotic Cells
14:29

Rapid In Vivo Fixation and Isolation of Translational Complexes from Eukaryotic Cells

Published on: December 25, 2021

4.9K
Toeprinting Analysis of Translation Initiation Complex Formation on Mammalian mRNAs
10:37

Toeprinting Analysis of Translation Initiation Complex Formation on Mammalian mRNAs

Published on: May 10, 2018

13.3K

Área de la Ciencia:

  • Biología molecular
  • Biología estructural
  • Biología celular

Sus antecedentes:

  • Las células eucariotas regulan la síntesis de proteínas durante el estrés inhibiendo el factor de iniciación de la traducción eucariota 2B (eIF2B).
  • eIF2B actúa como un factor de intercambio de nucleótidos de guanina para eIF2, crucial para iniciar la síntesis de proteínas.
  • La fosforilación inducida por el estrés de eIF2α inhibe la actividad de eIF2B, un mecanismo clave en el control traslacional.

Objetivo del estudio:

  • Determinar la estructura tridimensional del complejo eIF2B.
  • Aclarar la base estructural para la inhibición de eIF2B por eIF2α fosforilado.
  • Proporcionar un marco estructural para comprender el control traslacional inducido por el estrés.

Principales métodos:

  • Se utilizó la cristalografía de rayos X para determinar la estructura del complejo Schizosaccharomyces pombe eIF2B.
  • Análisis in vitro basado en la estructura, incluido el escaneo de la superficie y el enlace transversal dirigido al sitio, identificando las interfaces de unión.
  • Se construyó un modelo estructural del complejo eIF2α fosforilado por eIF2B.

Principales resultados:

  • La estructura cristalina reveló una disposición sin precedentes del heterodecámero eIF2B, con un subcomplejo regulador hexameric que une dos subcomplejos catalíticos.
  • Se identificaron las interfaces de unión eIF2α y eIF2γ en subcomplejos distintos.
  • El eIF2α fosforilado se une más fuertemente al eIF2B, formando un complejo no productivo que inhibe el intercambio de nucleótidos en el eIF2γ.

Conclusiones:

  • La estructura determinada proporciona una comprensión molecular detallada de la arquitectura eIF2B.
  • La fosforilación inducida por el estrés de eIF2α conduce a la formación de un complejo eIF2-eIF2B no productivo, deteniendo el intercambio de nucleótidos.
  • Este estudio ofrece una base estructural para la regulación mediada por eIF2B de la síntesis de proteínas bajo estrés celular.