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Videos de Conceptos Relacionados

Protein Folding01:25

Protein Folding

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Proteins are chains of amino acids linked together by peptide bonds. Upon synthesis, a protein folds into a three-dimensional conformation, critical to its biological function. Interactions between its constituent amino acids guide protein folding, and hence the protein structure is primarily dependent on its amino acid sequence.
Protein Structure Is Critical to Its Biological Function
Proteins perform a wide range of biological functions such as catalyzing chemical reactions, providing...
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Molecular Chaperones and Protein Folding03:00

Molecular Chaperones and Protein Folding

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The native conformation of a protein is formed by interactions between the side chains of its constituent amino acids. When the amino acids cannot form these interactions, the protein cannot fold by itself and needs chaperones. Notably, chaperones do not relay any additional information required for the folding of polypeptides; the native conformation of a protein is determined solely by its amino acid sequence. Chaperones catalyze protein folding without being a part of the folded protein.
The...
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Cotranslational Protein Translocation01:20

Cotranslational Protein Translocation

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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...
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Bacterial Protein Maturation01:26

Bacterial Protein Maturation

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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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Post-translational Translocation of Proteins to the RER01:27

Post-translational Translocation of Proteins to the RER

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A sizable fraction of proteins destined for ER are first synthesized in the cell cytosol and then transported across the ER membrane–a process called post-translational translocation. Similar to cotranslationally translocated proteins, these proteins also use the Sec translocon complex to enter the ER lumen.
Targeting proteins to the ER
Hsp40 and Hsp70 chaperone molecules bind the translated proteins in the cytosol to prevent their folding. The chaperone binding helps to keep the signal...
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Proteins: From Genes to Degradation02:11

Proteins: From Genes to Degradation

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Within a biological system, the DNA encodes the RNA, and the nucleotide sequence in the RNA further defines the amino acid sequence in the protein. This is referred to as “The Central Dogma of Molecular Biology” - a term coined by Francis Crick.  Central dogma is a firm principle in biology that defines the flow of genetic information within any life form. The two fundamental steps in central dogma are - transcription and translation.
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Video Experimental Relacionado

Updated: Sep 8, 2025

Analysis of Protein Folding, Transport, and Degradation in Living Cells by Radioactive Pulse Chase
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Analysis of Protein Folding, Transport, and Degradation in Living Cells by Radioactive Pulse Chase

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El plegamiento de proteínas co-translacionales a través de intermediarios estructurales no nativos

Siyu Wang1, Amir Bitran2, Ekaterina Samatova1

  • 1Department of Physical Biochemistry, Max Planck Institute for Multidisciplinary Sciences, Göttingen 37077, Germany.

Science advances
|September 5, 2025
PubMed
Resumen
Este resumen es generado por máquina.

Este estudio revela cómo se pliegan las proteínas a medida que se forman, identificando las interacciones clave que guían el proceso. Comprender este plegamiento cotranslacional es crucial para predecir el plegamiento erróneo de proteínas y diseñar nuevas proteínas.

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Área de la Ciencia:

  • Biología molecular
  • La biofísica
  • Biología computacional

Sus antecedentes:

  • El plegamiento de proteínas es esencial para la función celular, pero ocurre durante la traducción (plegamiento cotranslacional) dentro del ribosoma.
  • El plegamiento incorrecto, relacionado con enfermedades, surge de alteraciones en las vías de plegamiento cotranslacional.
  • Predecir estas vías a nivel atomístico sigue siendo un desafío significativo.

Objetivo del estudio:

  • Para predecir computacionalmente y validar experimentalmente los detalles atómicos de las vías de plegado cotranslacional.
  • Investigar el papel de las interacciones hidrofóbicas no nativas en la estabilización de los intermediarios de plegado temprano.
  • Comprender cómo el entorno del ribosoma y las chaperonas moleculares influyen en el plegamiento cotranslacional.

Principales métodos:

  • Simulaciones de dinámica molecular atómica para predecir las vías de plegado.
  • Validación experimental mediante técnicas biofísicas.
  • Análisis de las interacciones entre los péptidos nacientes y el túnel de salida del ribosoma.

Principales resultados:

  • Una jerarquía vectorial de plegado fue predicha computacionalmente y validada experimentalmente.
  • Los intermediarios de plegado temprano se estabilizan mediante interacciones hidrofóbicas transitorias y no nativas.
  • La interrupción de estas interacciones perjudica el plegamiento cotranslacional.
  • El factor de disparo de la chaperona modula la vía de plegamiento manteniendo la dinámica del péptido.

Conclusiones:

  • Los residuos expuestos a la superficie juegan un papel crítico, no reconocido previamente, en el plegamiento cotranslacional.
  • Los hallazgos proporcionan nuevas herramientas para mejorar la predicción del plegamiento de proteínas y el diseño de proteínas.
  • Este trabajo profundiza nuestra comprensión de los mecanismos fundamentales que rigen la biogénesis de las proteínas.